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    Биофизика для экологии и медицины: к 90-летию академика РАН И. И. Гительзона [Текст] / И. И. Гительзон, Т. Г. Волова, А. Г. Дегерменджи [и др.] ; ред., авт. предисл. Т. Г. Волова ; Российская академия наук, Сибирское отделение, Институт биофизики (Красноярск). - Новосибирск : Издательство Сибирского отделения Российской академии наук, 2019. - 292, [2] с. : ил., цв. ил. ; 25 см. - Рез. ст. англ. - Библиогр. в конце ст. - 300 экз. - ISBN 978-5-7692-1650-3 : 1635.00 р.
    Содержание:
Гительзон, Иосиф Исаевич. Краткий очерк истории, состояния и перспектив = A short essay on the history, state and prospects of the institute of biophysics FRC KSC SB RAS / И. И. Гительзон. - С .14-23
Медведева, С. Е. Коллекция культур ибсо как база для исследований биолюминесценции й и грибов в ИБФ СО РАН = Culture collection ibso as a basis for research of bioluminescence of bacteria and fungi in IBP SB RAS / С. Е. Медведева. - С .24-39. - Библиогр.: с. 37-39
Гительзон, Иосиф Исаевич. Биолюминесценция Мирового океана = Bioluminescence of the World Ocean / И. И. Гительзон, Л. А. Левин, А. С. Артемкин, Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П. Утюшев Р. Н. - С .40-60. - Библиогр.: с. 60
Другие авторы: Левин Л. А., Артемкин А. С., Утюшев Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П.
Кратасюк, В. А. Бактериальная люцифераза в биолюминесцентном анализе = Bacterial luciferase in bioluminescent analysis / В. А. Кратасюк, Е. Н. Есимбекова. - С .61-71. - Библиогр.: с. 70-71
Франк, Л. А. Целентеразин-зависимые биолюминесцентные системы = Coelenterazine-dependent bioluminescent systems / Л. А. Франк. - С .72-87. - Библиогр.: с. 85-87
Кл.слова: люцифераза
Пуртов, К. В. Изучение химического механизма биолюминесценции грибов = The study of the chemical mechanism of bioluminescence of fungi / К. В. Пуртов, В. Н. Петушков, Н. С. Родионова. - С .88-98. - Библиогр.: с. 98
Родионова, Н. С. Исследование биолюминесценции сибирских почвенных олигохет = Study of siberian bioluminescent earthworms / Н. С. Родионова, А. А. Петушков. - С .99-118. - Библиогр.: с. 116-118
Тихомиров, А. А. Экспериментальные модели замкнутых экосистем с расчетной долей человека как перспективное направление исследований по созданию биолого-технической системы жизнеобеспечения = Experimental models of closed ecosystems with the human calculated limits as a perspective direction of research on the creation of BTLSS / А. А. Тихомиров, С. А. Ушакова, Н. А. Тихомирова, С. В., Величко В. В. Трифонов С. В. - С .119-128. - Библиогр.: с. 128
Другие авторы: Ушакова С. А., Тихомирова Н. А., Трифонов С. В., Величко В. В.
Волова, Татьяна Григорьевна. Управляемый биосинтез: от параметрически управляемых продуцирующих биосистем до новейших биофизических технологий = Controlled biosynthesis: from parametrically controlled producing biosystems to newest biophysical technologies / Т. Г. Волова, Е. И. Шишацкая. - С .129-148. - Библиогр.: с. 147-148
Бондарь, Владимир Станиславович. Биомедицинские приложения наноалмазов взрывного синтеза = Biomedical applications of nanodiamonds of explosive synthesis / В. С. Бондарь, А. П. Пузырь, Н. О. Ронжин, А. В., Буров А. Е. Барон А. В. - С .149-165. - Библиогр.: с. 161-165
Другие авторы: Пузырь А. П., Ронжин Н. О., Барон А. В., Буров А. Е.
Болсуновский, Александр Яковлевич. Применение радиоизотопных методов в институте биофизики СО РАН: от клеток крови до экосистем = Use od radioisotope techniques in the Institute of Biophysics SB RAS: from blood cells to ecosystems / А. Я. Болсуновский, С. В. Косиненко, Т. А. Зотина, Д. В. Дементьев. - С .166-179. - Библиогр.: с. 177-179
Другие авторы: Косиненко С. В., Зотина Т. А., Дементьев Д. В.
Шевырногов, Анатолий Петрович. Биосфера - взгляд сверху (экспрессные методы мониторинга биосферы в ИБФ СО РАН – ХХ–ХХI вв.) = biosphere - a view from space (express methods of the biosphere monitoring in the Institute of Biophysics SB RAS – XX–XXI century) / А. П. Шевырногов. - С .180-193. - Библиогр.: с. 193
Гладышев, Михаил Иванович. Жирные кислоты в экологической биофизике водных систем = Fatty acids in ecological biophysics of aquatic ecosystems / М. И. Гладышев. - С .194-209. - Библиогр.: с. 206-209
Рогозин, Денис Юрьевич. Сравнительное исследование устойчивости стратификации и структуры трофической сети в меромиктических озерах Шира и Шунет (Южная Сибирь, Россия) = Comparative study of the stability of stratification and the food web structure in the meromictic lakes Shira and Shunet (South Siberia, Russia) / Д. Ю. Рогозин, Е. С. Задереев, И. Г. Прокопкин [и др.]. - С .210-247. - Библиогр.: с. 243-247
Другие авторы: Задереев Е. С., Прокопкин И. Г., Толомеев А. П., Бархатов Ю. В., Хромечек Е. Б., Дегерменджи Н. Н., Дроботов А. В., Дегерменджи А. Г.
Печуркин, Николай Савельевич. Непрерывный рост интенсивности энерго-вещественных взаимодействий в эволюции геобиосферы Земли = Transparent growth of the energy/matter interactions on Earth in the evolution of geobiosphere / Н. С. Печуркин, А. Н. Шуваев, Л. А. Сомова. - С .248-254
Барцев, Сергей Иванович. Малоразмерные модели биосферы и феноменология изменения глобального климата = Small-scale biosphere models and phenomenology of global climate change / С. И. Барцев, А. Г. Дегерменджи. - С .255-283. - Библиогр.: с. 281-283
Дегерменджи, Андрей Георгиевич. Направления развития биофизики в Красноярске / А. Г. Дегерменджи. - С .284-288

ГРНТИ	31.27	76.03
УДК	577	574	61

ББК Е071я43 + Р252.0я43
Рубрики:
Экологическая биофизика
Медицинская биофизика
Кл.слова (ненормированные):
биолюминесценция -- люцифераза -- целентаразин -- олигохеты -- замкнутые экосистемы -- управляемый биосинтез -- наноалмазы -- радиоизотопные методы -- биосфера -- жирные кислоты -- системы жизнеобеспечения -- меромиктические озера -- геобиосфера -- эволюция -- глобальный климат -- Медицинская биофизика
Аннотация: Сборник посвящен широкому кругу исследований в области экологической биофизики – научного направления на стыке наук – от исследований на молекулярном уровне до вопросов управления большими природными экосистемами. Рассмотрены исторические вехи развития экологического направления биофизики. Основной акцент сборника основан на современных, актуальных достижениях красноярских биофизиков, которым удалось сохранить и развить многоплановые направления, которые были заложены в 50-х гг. ХХ века И. И. Гительзоном. Наряду с обзорными материалами и результатами фундаментальных исследований представлен ряд готовых к внедрению биотехнологий. Книга адресована биофизикам, экологам и химикам, а также преподавателям и студентам биофизических, биологических и экологических кафедр университетов.

Держатели документа:
Библиотека Института биофизики СО РАН : 660036, Академгородок, 50/12

Доп.точки доступа:
Гительзон, Иосиф Исаевич; Волова, Татьяна Григорьевна; Дегерменджи, Андрей Георгиевич; Дегерменджи, Н. Н.; Шевырногов, Анатолий Петрович; Кратасюк, В. А.; Барцев, Сергей иванович; Болсуновский, Александр Яковлевич; Бондарь, Владимир Антонович; Буров, А. Е.; Величко, В. В.; Гладышев, Михаил Иванович; Есимбекова, Е. Н.; Дементьев, Д. В.; Задереев, Егор Сергеевич; Зотина, Т. А.; Косиненко, Сергей Васильевич; Медведева, С. Е.; Петушков, В. Н.; Печуркин, Николай Савельевич; Прокопкин, И. Г.; Пузырь, А. П.; Пуртов, К. В.; Рогозин, Денис Юрьевич; Родионова, Н. С.; Ронжин, Н. О.; Сомова, Лидия Александровна; Тихомиров, Александр Аполлинариевич; Тихомирова, Наталья Александровна; Трифонов, С. В.; Ушакова, Софья Аврумовна; Франк, Л. А.; Хромечек, Е. Б.; Шишацкая, Е. И.; Шуваев, А. Н.; Волова, Татьяна Григорьевна \ред., авт. предисл.\; Утюшев Р. Н., Чепилов В. В., Молвинских С.Л., Черепанов О. А., Чугунов Ю. В., Караев Н. Д., Загородний Ю. А., Шевырногов А. П.; Трифонов С. В., Величко В. В.; Барон А. В., Буров А. Е.; Толомеев А. П., Бархатов Ю. В., Хромечек Е. Б., Дегерменджи Н. Н.; Дроботов А. В.; Дегерменджи А. Г., Андрей Георгиевич; Гительзон, Иосиф Исаевич \о нем\; Российская академия наук. Сибирское отделение; Институт биофизики (Красноярск)
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Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobiol.2017.07.021 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenteramide -- Coelenterazine -- Cysteine -- Photoprotein -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or ?-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coli, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild-type aequorin. In contrast, Cys-free obelin retains only ~ 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a “fast” component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 ± 0.2 and 44.6 ± 0.4 °C for aequorin and Cys-free aequorin, and 49.1 ± 0.1 and 28.8 ± 0.3 °C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield. © 2017 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Eremeeva, E. V.; Vysotski, E. S.

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Bioluminescent and biochemical properties of Cys-free Ca2+-regulated photoproteins obelin and aequorin / E. V. Eremeeva, E. S. Vysotski // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 174. - P97-105, DOI 10.1016/j.jphotobio1.2017.07.021. - Cited References:54. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 03562016-0712 and 0356-2015-0103) and the RFBR grant 17-04-00764. . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
SEQUENCE-ANALYSIS
   APO-OBELIN
   INTRINSIC FLUORESCENCE
   COELENTERAZINE
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Coelenteramide -- Cysteine -- Serine
Аннотация: Bioluminescence of a variety of marine coelenterates is determined by Ca2+-regulated photoproteins. A strong interest in these proteins is for their wide analytical potential as intracellular calcium indicators and labels for in vitro binding assays. The presently known hydromedusan Ca2+-regulated photoproteins contain three (aequorin and clytin) or five (obelin and mitrocomin) cysteine residues with one of them strictly conserved. We have constructed Cys-free aequorin and obelin by substitution of all cysteines to serine residues. Such mutants should be of interest for researchers by the possibility to avoid the incubation with dithiothreitol (or p-mercaptoethanol) required for producing an active photoprotein that is important for some prospective analytical assays in which the photoprotein is genetically fused with a target protein sensitive to the reducing agents. Cys-free mutants were expressed in Escherichia coil, purified, and characterized regarding the efficiency of photoprotein complex formation, functional activity, and conformational stability. The replacement of cysteine residues has been demonstrated to affect different properties of aequorin and obelin. Cys-free aequorin displays a two-fold lower specific bioluminescence activity but preserves similar activation properties and light emission kinetics compared to the wild -type aequorin. In contrast, Cys-free obelin retains only 10% of the bioluminescence activity of wild-type obelin as well as binding coelenterazine and forming active photoprotein much less effectively. In addition, the substitution of Cys residues drastically changes the bioluminescence kinetics of obelin completely eliminating a "fast" component from the light signal decay curve. At the same time, the replacement of Cys residues increases conformational flexibility of both aequorin and obelin molecules, but again, the effect is more prominent in the case of obelin. The values of thermal midpoints of unfolding (Tm) were determined to be 53.3 0.2 and 44.6 0.4 C for aequorin and Cys-free aequorin, and 49.1 0.1 and 28.8 0.3 C for obelin and Cys-free obelin, respectively. Thus, so far only Cys-free aequorin is suitable as a partner for fusing with a tag sensitive to reducing agents since the aequorin mutant preserves almost 50% of the bioluminescent activity and can be produced with a substantial yield.

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Держатели документа:
RAS, Photobiol Lab, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,SB, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Academy of Sciences [03562016-0712, 0356-2015-0103]; RFBR [17-04-00764]

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Bioluminescent detection of tick-borne encephalitis virus in native ticks / A. N. Kudryavtsev, L. P. Burakova, L. A. Frank // Anal. Methods. - 2017. - Vol. 9, Is. 15. - P2252-2255, DOI 10.1039/c7ay00535k . - ISSN 1759-9660
Кл.слова (ненормированные):
Proteins -- Recombinant proteins -- Viruses -- Binding proteins -- Bioluminescence
Аннотация: A one-step bioluminescent immunoassay for tick-borne encephalitis virus (TBEV) in natural ticks based on the hybrid protein 14D5a-Rm7 was developed. Recombinant Ca2+-dependent coelenterazine-binding protein was shown to be a more convenient substrate form for the Rm7 domain than coelenterazine. Over 600 samples of natural ticks were analyzed and shown to have essential differences in the discrimination factor D for TBEV-positive (2.77 ± 0.81) and TBEV-negative (1.15 ± 0.28) samples. © The Royal Society of Chemistry.

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kudryavtsev, A. N.; Burakova, L. P.; Frank, L. A.

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The novel extremely psychrophilic luciferase from Metridia longa: Properties of a high-purity protein produced in insect cells / M. D. Larionova, S. V. Markova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 2017. - Vol. 483, Is. 1. - P772-778, DOI 10.1016/j.bbrc.2016.12.067. - Cited References:24. - The cloning of cDNAs encoding MLuc2 isoforms of M. longa was supported by Bayer AG (Germany) and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 01201351504); all other studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
EXPRESSION
ENZYME
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Bioluminescent reporter -- Psychrophilic -- enzyme -- Molecular adaptation
Аннотация: The bright bioluminescence of copepod Metridia longa is conditioned by a small secreted coelenterazinedependent luciferase (MLuc). To date, three isoforms of MLuc differing in length, sequences, and some properties were cloned and successfully applied as high sensitive bioluminescent reporters. In this work, we report cloning of a novel group of genes from M. longa encoding extremely psychrophilic isoforms of MLuc (MLuc2-type). The novel isoforms share only similar to 54-64% of protein sequence identity with the previously cloned isoforms and, consequently, are the product of a separate group of paralogous genes. The MLuc2 isoform with consensus sequence was produced as a natively folded protein using baculovirus/ insect cell expression system, purified, and characterized. The MLuc2 displays a very high bioluminescent activity and high thermostability similar to those of the previously characterized M. longa luciferase isoform MLuc7. However, in contrast to MLuc7 revealing the highest activity at 12-17 degrees C and 0.5 M NaCl, the bioluminescence optima of MLuc2 isoforms are at similar to 5 degrees C and 1 M NaCl. The MLuc(2) adaptation to cold is also accompanied by decrease of melting temperature and affinity to substrate suggesting a more conformational flexibility of a protein structure. The luciferase isoforms with different temperature optima may provide adaptability of the M. longa bioluminescence to the changes of water temperature during diurnal vertical migrations. (C) 2016 Elsevier Inc. All rights reserved.

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Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Academy of Sciences [01201351504]; RFBR; Government of Krasnoyarsk Territory [16-44-242099]

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Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa / M. D. Larionova, S. V. Markova, E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P503-510, DOI 10.1111/php.12694. - Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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Shining Light on the Secreted Luciferases of Marine Copepods: Current Knowledge and Applications. / S. V. Markova, M. D. Larionova, E. S. Vysotski // Photochemistry and photobiology. - 2018, DOI 10.1111/php.13077 . - ISSN 1751-1097
Аннотация: Copepod luciferases - a family of small secretory proteins of 18.4-24.3 kDa, including a signal peptide, are responsible for bright secreted bioluminescence of some marine copepods. The copepod luciferases use coelenterazine as a substrate to produce blue light in a simple oxidation reaction without any additional cofactors. They do not share sequence or structural similarity with other identified bioluminescent proteins including coelenterazine-dependent Renilla and Oplophorus luciferases. The small size, strong luminescence activity and high stability, including thermostability, make secreted copepod luciferases very attractive candidates as reporter proteins which are particularly useful for nondisruptive reporter assays and for high-throughput format. The most known and extensively investigated representatives of this family are the first cloned GpLuc and MLuc luciferases from copepods Gaussia princeps and Metridia longa, respectively. Immediately after cloning these homologous luciferases were successfully applied as bioluminescent reporters in vivo and in vitro, and since then the scope of their applications continues to grow. This review is an attempt to systemize and critically evaluate the data scattered through numerous articles regarding the main structural features of copepod luciferases, their luminescent and physicochemical properties. We also review the main trends of their application as bioluminescent reporters in cell and molecular biology. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center "Krasnoyarsk Science Center SB RAS", Krasnoyarsk, 660036, Russia.
Siberian Federal University, Krasnoyarsk, 660041, Russia.
N.N. Blokhin National Medical Research Center of Oncology, Ministry of Health of Russia, Moscow, 115478, Russia.

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Vysotski, Eugene S.

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Exploring Bioluminescence Function of the Ca2+-regulated Photoproteins with Site-directed Mutagenesis / E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. - 2019. - Vol. 95, Is. 1. - P8-23, DOI 10.1111/php.12945. - Cited References:88. - This work was supported by grant 17-04-00764 of Russian Foundation for Basic Research and the state budgetallocated to the fundamental research at the Russian Academy of Sciences (project 0356-2017-0017). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-BINDING PHOTOPROTEIN
GREEN-FLUORESCENT PROTEIN
JELLYFISH
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- aequorin -- obelin -- clytin -- mitrocomin -- EF-hand protein
Аннотация: Site-directed mutagenesis is a powerful tool to investigate the structure-function relationship of proteins and a function of certain amino acid residues in catalytic conversion of substrates during enzymatic reactions. Hence, it is not surprising that this approach was repeatedly applied to elucidate the role of certain amino acid residues in various aspects of photoprotein bioluminescence, mostly for aequorin and obelin, and to design mutant photoproteins with altered properties (modified calcium affinity, faster or slower bioluminescence kinetics, different emission color) which would either allow the development of novel bioluminescent assays or improvement of characteristics of the already existing ones. This information, however, is scattered over different articles. In this review, we systematize the findings that were made using site-directed mutagenesis studies regarding the impact of various amino acid residues on bioluminescence of hydromedusan Ca2+-regulated photoproteins. All key residues that have been identified are pinpointed, and their influence on different aspects of photoprotein functioning such as active photoprotein complex formation, bioluminescence reaction, calcium response and light emitter formation is discussed.

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RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr,Photobiol Lab, Krasnoyarsk, Russia.

Доп.точки доступа:
Eremeeva, Elena V.; Vysotski, Eugene S.; Russian Foundation for Basic Research [17-04-00764]; Russian Academy of Sciences [0356-2017-0017]

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Hydrogen bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine determines the bioluminescence spectra differences among hydromedusan calcium-regulated photoproteins / E. Vysotski [et al.] // FEBS Open Bio. - 2018. - Vol. 8. - P435-436. - Cited References:0. - This work was supported by RFBR grant 17-04-00764 and a China-Russia international collaboration grant from the Chinese Academy of Sciences and the Natural Science Foundation of China. . - ISSN 2211-5463

РУБ Biochemistry & Molecular Biology

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Photobiol Lab, Inst Biophys SB RAS, Krasnoyarsk, Russia.
ShanghaiTech Univ, IHuman Inst, Shanghai, Peoples R China.
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA.
Доп.точки доступа:
Vysotski, E.; Markova, S.; Natashin, P.; Stepanyuk, G.; Lee, J.; Malikova, N.; Liu, Z.; RFBR [17-04-00764]; China-Russia international collaboration grant from Chinese Academy of Sciences; Natural Science Foundation of China

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10.

The disulfide-rich Metridia luciferase refolded from E. coli inclusion bodies reveals the properties of a native folded enzyme produced in insect cells / S. V. Markova [et al.] // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 175. - P51-57, DOI 10.1016/j.jphotobiol.2017.08.024. - Cited References:30. - These studies were funded by RFBR and the Government of Krasnoyarsk Territory according to the research project No. 16-44-242099 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 0356-2016-0712). . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GAUSSIA-PRINCEPS LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
   PROTEIN
Кл.слова (ненормированные):
Copepod luciferase -- Disulfide bonds -- Cysteine-rich protein -- Oxidative -- refolding
Аннотация: The bioluminescence of a marine copepod Metridia Tonga is determined by a small secreted coelenterazine-dependent luciferase that uses coelenterazine as a substrate of enzymatic reaction to generate light (lambda(max) = 480 nm). To date, four different isoforms of the luciferase differing in size, sequences, and properties have been cloned by functional screening. All of them contain ten conserved Cys residues that suggests up to five S-S intramolecular bonds per luciferase molecule. Whereas the use of copepod luciferases as bioluminescent reporters in biomedical research in vivo is growing from year to year, their application for in vitro assays is still limited by the difficulty in obtaining significant amounts of luciferase. The most cost-effective host for producing recombinant proteins is Escherichia coli. However, prokaryotic and eukaryotic cells maintain the reductive environment in cytoplasm that hinders the disulfide bond formation and consequently the proper folding of luciferase. Here we report the expression of the MLuc7 isoform of M. longa luciferase in E. colt cells and the efficient procedure for refolding from inclusion bodies yielding a high-active monomeric protein. Furthermore, in a set of identical experiments we demonstrate that bioluminescent and structural features of MLuc7 produced in bacterial cells are identical to those of MLuc7 isoform produced from culture medium of insect cells. Although the yield of high-purity protein is only 6 mg/L, the application of E. coil cells to produce the luciferase is simpler and more cost-effective than the use of insect cells. We expect that the suggested technology of Metridia luciferase production allows obtaining of sufficient amounts of protein both for the development of novel in vitro analytical assays with the use of MLuc7 as a label and for structural studies.

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RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Photobiol Lab,Inst Biophys SB, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Gorbunova, Darya A.; Vysotski, Eugene S.; RFBR; Government of Krasnoyarsk Territory [16-44-242099]; Russian Academy of Sciences [0356-2016-0712]

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11.

Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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12.

Bioluminescent detection probe for tick-borne encephalitis virus immunoassay [Text] / L. P. Burakova [et al.] // Anal. Bioanal. Chem. - 2015. - Vol. 407, Is. 18. - P5417-5423, DOI 10.1007/s00216-015-8710-6. - Cited References:19. - The work was supported by the Russian Academy of Sciences, Siberian Branch, within the framework of the Interdisciplinary Integration Project No. 139 and the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1). . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
COELENTERAZINE-BINDING PROTEIN
ENZYME-IMMUNOASSAY
RENILLA-MUELLERI
Кл.слова (ненормированные):
Tick-borne encephalitis virus -- Single-chain antibody -- Luciferase -- Immunoassay
Аннотация: To facilitate the detection of the tick-borne encephalitis virus (TBEV), the causative agent of one of the most severe human neuroinfections, we have developed an immunoassay based on bioluminescent hybrid protein 14D5a-Rm7 as a detection probe. The protein containing Renilla luciferase as a reporter and a single-chain variable fragment (scFv) of murine immunoglobulin to TBEV as a recognition element was constructed, produced by bacterial expression, purified, and tested. Both domains were shown to reveal their specific biological properties-affinity to the target antigen and bioluminescent activity. Hybrid protein was applied as a label for solid-phase immunoassay of the antigens, associated with the tick-borne encephalitis virus (native glycoprotein E or extracts of the infected strain of lab ticks). The assay demonstrates high sensitivity (0.056 ng of glycoprotein E; 10(4)-10(5) virus particles or 0.1 pg virions) and simplicity and is competitive with conventional methods for detection of TBEV.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Poliomyelitis & Viral Encephalitides, Moscow 142782, Russia.
Res Inst Nat Foci Infect, Omsk 644080, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Kudryavtsev, Alexander N.; Stepanyuk, Galina A.; Baykov, Ivan K.; Morozova, Vera V.; Tikunova, Nina V.; Dubova, Maria A.; Lyapustin, Victor N.; Yakimenko, Valeri V.; Frank, Ludmila A.; Russian Academy of Sciences, Siberian Branch [139]; Russian Academy of Sciences [VI 57.1.1]

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13.

Coelenterazine-dependent luciferases / S. V. Markova, E. S. Vysotski // Biochemistry Moscow. - 2015. - Vol. 80, Is. 6. - P714-732, DOI 10.1134/S0006297915060073 . - ISSN 0006-2979
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- luciferin -- Coelenterata -- Cypridina luciferin -- Fungi -- Hexapoda -- Mollusca -- Protozoa
Аннотация: Bioluminescence is a widespread natural phenomenon. Luminous organisms are found among bacteria, fungi, protozoa, coelenterates, worms, molluscs, insects, and fish. Studies on bioluminescent systems of various organisms have revealed an interesting feature - the mechanisms underlying visible light emission are considerably different in representatives of different taxa despite the same final result of this biochemical process. Among the several substrates of bioluminescent reactions identified in marine luminous organisms, the most commonly used are imidazopyrazinone derivatives such as coelenterazine and Cypridina luciferin. Although the substrate used is the same, bioluminescent proteins that catalyze light emitting reactions in taxonomically remote luminous organisms do not show similarity either in amino acid sequences or in spatial structures. In this review, we consider luciferases of various luminous organisms that use coelenterazine or Cypridina luciferin as a substrate, as well as modifications of these proteins that improve their physicochemical and bioluminescent properties and therefore their applicability in bioluminescence imaging in vivo. © 2015 Pleiades Publishing, Ltd.

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Держатели документа:
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Markova, S.V.; Vysotski, E.S.

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14.

The smallest natural high-active luciferase: Cloning and characterization of novel 16.5-kDa luciferase from copepod Metridia longa [Text] / S. V. Markova [et al.] // Biochem. Biophys. Res. Commun. - 2015. - Vol. 457, Is. 1. - P77-82, DOI 10.1016/j.bbrc.2014.12.082. - Cited References:20. - The cloning of cDNA encoding MLuc7 luciferase of M. longa was supported by Bayer AG (Germany); all other studies - by the grant 14-14-01119 of the Russian Science Foundation. We declare that authors have no conflict of interest. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
   SECRETED LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Mammalian -- expression -- Real-time imaging
Аннотация: Coelenterazine-dependent copepod luciferases containing natural signal peptide for secretion are a very convenient analytical tool as they enable monitoring of intracellular events with high sensitivity, without destroying cells or tissues. This property is well suited for application in biomedical research and development of cell-based assays for high throughput screening. We report the cloning of cDNA gene encoding a novel secreted non-allelic 16.5-kDa isoform (MLuc7) of Metridia longa luciferase, which, in fact, is the smallest natural luciferase of known for today. Despite the small size, isoform contains 10 conservative Cys residues suggesting the presence of up to 5 S-S bonds. This hampers the efficient production of functionally active recombinant luciferase in bacterial expression systems. With the use of the baculovirus expression system, we produced substantial amounts of the proper folded MLuc7 luciferase with a yield of similar to 3 mg/L of a high purity protein. We demonstrate that MLuc7 produced in insect cells is highly active and extremely thermostable, and is well suited as a secreted reporter when expressed in mammalian cells ensuring higher sensitivity of detection as compared to another Metridia luciferase isoform (MLuc164) which is widely employed in real-time imaging. (C) 2014 Elsevier Inc. All rights reserved.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.
ИБФ СО РАН

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Burakova, Ludmila P.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Science Foundation [14-14-01119]

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15.

Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration [Text] / N. P. Malikova [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5715-5726, DOI 10.1007/s00216-014-7986-2. - Cited References: 67. - This work was supported by RFBR grant 12-04-00131, by the programs of the Government of the Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) and "Molecular and Cellular Biology" of the Russian Academy of Sciences, and the grant from the President of the Russian Federation "Leading Science School" (3951.2012.4). . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
   CTENOPHORE BEROE ABYSSICOLA
   GREEN-FLUORESCENT PROTEIN
   INTRACELLULAR CALCIUM
   SEQUENCE-ANALYSIS
   CA-2+-ACTIVATED PHOTOPROTEIN
   CA2+-BINDING PHOTOPROTEIN
   SEMISYNTHETIC AEQUORINS
   LUMINESCENT PROTEIN
   RECOMBINANT OBELIN
Кл.слова (ненормированные):
Calcium -- Coelenterazine -- Aequorin -- Obelin -- Clytin -- Mitrocomin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y(2) receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration.

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Держатели документа:
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Burakova, L.P.; Markova, S.V.; Vysotski, E.S.; RFBR [12-04-00131]; Government of the Russian Federation [11.G34.31.0058]; Russian Academy of Sciences; Russian Federation "Leading Science School" [3951.2012.4]

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16.

Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course [Text] / N. G. Berestovskaya [et al.] // Anal. Biochem. - 1999. - Vol. 268, Is. 1. - P. 72-78, DOI 10.1006/abio.1998.3051. - Cited References: 22 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
Рубрики:
SEQUENCE-ANALYSIS
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   LIGHT-EMISSION
   AEQUORIN
   CDNA
   CLONING
   EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.

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Держатели документа:
Russian Acad Sci, Branch Inst Bioorgan Chem, Pushchino 142292, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Tech Univ Berlin, Inst Biochem & Mol Biol, D-10587 Berlin, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Berestovskaya, N.G.; Shaloiko, L.A.; Gorokhovatsky, A.Y.; Bondar, V.S.; Vysotski, E.S.; Maximov, J.E.; von Doehren, H...; Alakhov, Y.B.

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17.

Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria [Text] / E. V. Eremeeva, E. S. van Berkel, E. S. Vysotski // FEBS Lett. - 2016. - Vol. 590, Is. 3. - P307-316, DOI 10.1002/1873-3468.12052. - Cited References:34. - This study was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0014-5793. - ISSN 1873-3468

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
ENERGY-TRANSFER
CA2+-REGULATED
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine -- FRET -- obelin -- protein-protein -- interaction
Аннотация: Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Wageningen Univ, Biochem Lab, NL-6700 AP Wageningen, Netherlands.

Доп.точки доступа:
Eremeeva, Elena V.; van Berkel, Willem J. H.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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18.

Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin / L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2016. - Vol. 15, Is. 5. - P691-704, DOI 10.1039/c6pp00050a . - ISSN 1474-905X
Аннотация: Bright bioluminescence of ctenophores is caused by Ca2+-regulated photoproteins. Although these photoproteins are functionally identical to and share many properties of cnidarian photoproteins, like aequorin and obelin, and retain the same spatial architecture, they are extremely sensitive to light, i.e. lose the ability to bioluminesce on exposure to light over the entire absorption spectrum. In addition, the degree of identity of their amino acid sequences with those of cnidarian photoproteins is only 29.4%. This suggests that the residues involved in bioluminescence of ctenophore and cnidarian photoproteins significantly differ. Here we describe the bioluminescent properties of berovin mutants with substitution of the residues located in the photoprotein internal cavity. Since the spatial structure of berovin bound with a substrate is not determined yet, to identify these residues we have modeled it with an accommodated substrate using the structures of some cnidarian Ca2+-regulated photoproteins with bound coelenterazine or coelenteramide as templates in order to obtain an adequate sampling and to take into account all possible conformers and variants for ligand-protein docking. Based on the impact of substitutions on the bioluminescent properties and model structures we speculate that within the internal cavity of ctenophore photoproteins, coelenterazine is bound as a 2-peroxy anion adduct which is stabilized owing to Coulomb interaction with a positively charged guanidinium group of Arg41 paired with Tyr204. In this case, the bioluminescence reaction is triggered by only calcium-induced conformational changes leading to the disturbance of charge-charge interaction. © 2016 The Royal Society of Chemistry and Owner Societies.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Stepanyuk, G. A.; Eremeeva, E. V.; Vysotski, E. S.

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19.

All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

Scopus,
WOS
Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
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20.

Creation of Artificial Luciferases to Expand their Analytical Potential [Text] / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929, DOI 10.2174/1386207318666150917100011. - Cited References:79. - The work was supported by: the RFBR grant No. 14-08-00902/14; the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1). . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
BIOLUMINESCENT REPORTER APPLICATIONS
COELENTERAZINE-BINDING PROTEIN
Кл.слова (ненормированные):
Luciferase -- luciferin -- photoprotein -- bioluminescence -- mutagenesis -- luciferase-based assay -- bioimaging -- reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescence-based analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Frank, Ludmila A.; RFBR [14-08-00902/14]; [VI 57.1.1]

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