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Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Вербов В.Н., Высоцкий Е.С., Бондарь В.С., Артюхов А.И., Летунов В.Н., Мартюшин С.В.
Заглавие : Использование Ca-зависимого фотопротеина обелина в качестве метки в иммунолюминесцентном анализе : научное издание
Место публикации : Актуал. вопр. мед. биотехнол.: Матер. науч. конф., посвящ. 85-летию Том. НИИ вакцине и сывороток НПО "Вирион". - Томск, 1991. - Ч. 2. - С. 39-40
ГРНТИ : 62.41.09
Предметные рубрики: БЕЛОК
ФОТОБЕЛОК
ОБЕЛИН
CA-ЗАВИСИМЫЙ
СОЕДИНЕНИЯ-МЕТКА
ИММУНОХИМИЧЕСКАЯ РЕАКЦИЯ
ИСПОЛЬЗОВАНИЕ
OBELIA LONGISSIMA
PHOTOPROTEIN
Аннотация: В процессе поиска соединений-меток, к-рые при иммунохимической реакции обеспечивают более высокую чувствительность иммунологического анализа, был изучен фотобелок обелин, выделенный из экстрактов люминесцирующего гидроида Obelia longissima. Обелин, взаимодействуя с ионами кальция, способен испускать 4,5* *10{1}{5} кванта света на 1 мг белка, что позволяет обнаружить до 10{-}{2}{0}-10{-}{2}{1} Моль в-ва метки. Россия, НИИ Вакцин и сывороток НПО "Вирион", г. Томск.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Высоцкий, Евгений Степанович, Бондарь, Владимир Станиславович, Гительзон, Иосиф Исаевич
Заглавие : Выделение и свойства различных молекулярных форм Ca{2}{+}-активируемого фотопротеина обелина : научное издание
Место публикации : Докл. АН СССР. - 1991. - Т. 321, N 1. - С. 214-217. - ISSN 0002-3264
ГРНТИ : 31.23.27
Предметные рубрики: ФОТОПРОТЕИН
CA-АКТИВИРУЕМЫЙ
ОБЕЛИН
ВЫДЕЛЕНИЕ
СВОЙСТВА
CA-ACTIVATED PHOTOPROTEIN
OBELIN
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Высоцкий Е.С., Бондарь В.С., Летунов В.Н.
Заглавие : Выделение и очистка Ca-зависимого фотопротеина - обелина из гидроидных полипов Obelia longissima : научное издание
Место публикации : Биохимия. - 1989. - Т. 54, N 6. - С. 965-973. - ISSN 0320-9725
ГРНТИ : 31.23.27
Предметные рубрики: ФОТОПРОТЕИН
КАЛЬЦИЙ-ЗАВИСИМЫЙ
ОБЕЛИН
ВЫДЕЛЕНИЕ
ОЧИСТКА
OBELIA LONGISSIMA
ПОЛИПЫ ГИДРОИДНЫЕ
OBELIN
CA-ACTIVATED PHOTOPROTEIN
EXTRACTION/PURIFICATION
HYDROID POLYPS
BIOLUMINESCENCE
Аннотация: Описан способ выделения и очистки Ca-зависимого фотопротеина - обелина из гидроидных полипов Obelia longissima, включающий: разрушение материала в гипотонич. буфере, фракционирование ПЭГ 6000, фракционирование (NH[4])[2]SO[4] в диапазоне 40-75% насыщения, хроматографию на ДЭАЭ-целлюлозе DE-52, хроматографию на фенил-сефарозе 4В, гель-фильтрацию на сефадексе G-75, гель-фильтрацию на колонке Superose 12 HR 10/30 при помощи системы FPLC. С помощью предложенного метода получен практически чистый обелин с выходом 30-40%. Мол. м. полученного белка, определенная гель-фильтрацией в неденатурирующих условиях, составляет 39,6 кДа, тогда как электрофорез в полиакриламидном геле с додецилсульфатом натрия показывал наличие двух белков с мол. м. 27 и 15,6 кДа соответственно. Библ. 28. Ин-т биофизики СО АН СССР, Красноярск, СССР
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Бондарь В.С., Трофимов К.П., Высоцкий Е.С.
Заглавие : Физико-химические свойства фотопротеина из гидроидного полипа Obelia longissima : научное издание
Место публикации : Биохимия. - 1992. - Т. 57, N 10. - С. 78. - ISSN 0320-9725
ГРНТИ : 31.23.27
Предметные рубрики: ФОТОПРОТЕИНЫ
ФИЗИКО-ХИМИЧЕСКИЕ СВОЙСТВА
ГИДРОИДНЫЕ ПОЛИПЫ
PHOTOPROTEIN PROPERTIES
Аннотация: Из гидроидов вида Obelia longissima по схеме, включающей гель-фильтрацию на Сефадексе G-75 (fine), ИОХ на Полисил СА-300 (10 мкм), гидрофобную хр-фию на фенил-Сефарозе CL-4В, гель-фильтрацию на Сефакриле S-200 (Superfine), ИОХ на колонке Mono Q при pH 7,0, хроматофокусирввание на колонке MonoP (градиент pH 6,0-4,0) ИОХ на колонке Mono Q при pH 5,5; 8,8; 7,0 выделен гомогенный (по данным ЭФ с DDC-Na) фотопротеин обелин. Мол. м. белка в нативных условиях составляет 30 кД, в присутствии DDC-Na-19,8 кД. Уд. акт. обелина равна 4,9*10{1}{5} квант на 1 мг белка; константа псевдопер.З064 вого порядка спада биолюминесценции - 4 с{-}{1}; квантовый выход - 0,16. Интервал измерения ионов кальция составляет 10{-}{7}-10{-}{5} М. Для обелина характерен спектр люминесценции с максимумом при 469 нм, спектральный максимум флуоресценции разряженного фотопротеина находится при 455 нм. Оптимум pH люминесценции обелина приходится на интервал 9,0-10,5. Молек. константы ионизации имеют значения pK[1] 6,8 и pK[2] 12,2; константы ионизации для активного центра - pK[1] 9,1 и pK[2] 10,2 соотв. Библ. 36. Россия, ин-т биофизики СО РАН, Красноярск.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Liu Z.J., Markova S.V., Blinks J.R., Deng L..., Frank L.A., Herko M..., Malikova N.P., Rose J.P., Wang B.C., Lee J...
Заглавие : Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species
Колич.характеристики :12 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2003. - Vol. 42, Is. 20. - С. 6013-6024. - ISSN 0006-2960, DOI 10.1021/bi027258h
Примечания : Cited References: 45
Предметные рубрики: RAY CRYSTALLOGRAPHIC ANALYSIS
PHOTOPROTEIN AEQUORIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CALCIUM
LUMINESCENCE
LONGISSIMA
EVOLUTION
PROTEINS
COELENTERAZINE
Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Borisova V.V., Markova S.V., Malikova N.P., Stepanyuk G.A., Vysotski E.S.
Заглавие : Violet and greenish photoprotein obelin mutants for reporter applications in dual-color assay
Колич.характеристики :6 с
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2008. - Vol. 391, Is. 8. - С. 2891-2896. - ISSN 1618-2642, DOI 10.1007/s00216-008-2223-5
Примечания : Cited References: 22
Предметные рубрики: ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
BIOLUMINESCENCE
AEQUORIN
IMMUNOASSAY
EXPRESSION
CDNA
PURIFICATION
CLONING
Ключевые слова (''Своб.индексиров.''): ca(2+)-regulated photoprotein--bioluminescence--dual-color assay
Аннотация: Two kinds of Ca(2+)-regulated photoprotein obelin with altered color of bioluminescence were obtained by active-center amino acid substitution. The mutant W92F-H22E emits violet light (lambda(max)=390 nm) and the mutant Y139F emits greenish light (lambda (max)=498 nm), with small spectral overlap, both display high activity and stability and thus may be used as reporters. For demonstration, the mutants were applied in dual-color simultaneous immunoassay of two gonadotropic hormones-follicle-stimulating hormone and luteinizing hormone. Bioluminescence of the reporters was simultaneously triggered by single injection of Ca(2+) solution, divided using band-pass optical filters and measured with a two-channel photometer. The sensitivity of simultaneous bioluminescence assay was close to that of a separate radioimmunoassay.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Illarionova V.A., Vysotski E.S.
Заглавие : Use of proZZ-obelin fusion protein in bioluminescent immunoassay
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1996. - Vol. 219, Is. 2. - С. 475-479. - 5. - ISSN 0006-291X, DOI 10.1006/bbrc.1996.0258
Примечания : Cited References: 21
Предметные рубрики: ESCHERICHIA-COLI
EXPRESSION
AEQUORIN
PURIFICATION
SYSTEM
Аннотация: Obelin is a photoprotein that emits light by Ca2+-binding. To develop a bioluminescent immunoassay based on the light emission property of obelin, we have expressed the apoobelin fusion protein with ZZ-domain of S. aureus protein A in E. coil by recombinant DNA techniques. The pro2Z-obelin expressed was purified by one-step affinity chromatography on IgG-Agarose. The purified proZZ-obelin has both the luminescent activity of obelin and the IgG-binding ability of ZZ-domain. The specific activity of fusion protein was 8.5 x 10(15) photons per mg of protein. (C) 1996 Academic Press, Inc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tomilin F. N., Rogova A. V., Burakova L. P., Tchaikovskaya O. N., Avramov P. V., Fedorov D. G., Vysotski E. S.
Заглавие : Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory
Место публикации : Photochem. Photobiol. Sci.: Springer Nature, 2021. - Vol. 20, Is. 4. - С. 559-570. - ISSN 1474905X (ISSN), DOI 10.1007/s43630-021-00039-5
Аннотация: Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460–470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein–substrate complex was optimized using a linear scaling quantum–mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60° of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified. © 2021, The Author(s), under exclusive licence to European Photochemistry Association,European Society for Photobiology.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tomilin, Felix N., Rogova, Anastasia V., Burakova, Ludmila P., Tchaikovskaya, Olga N., Avramov, Pavel V., Fedorov, Dmitri G., Vysotski, Eugene S.
Заглавие : Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory
Колич.характеристики :12 с
Коллективы : RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]; NSFCNational Natural Science Foundation of China (NSFC) [19-54-53004]; Russian Ministry of Science and EducationMinistry of Education and Science, Russian Federation [0721-2020-0033]
Место публикации : Photochem. Photobiol. Sci.: SPRINGERNATURE, 2021. - Vol. 20, Is. 4. - С. 559-570. - ISSN 1474-905X, DOI 10.1007/s43630-021-00039-5. - ISSN 1474-9092(eISSN)
Примечания : Cited References:61. - The ab initio quantum chemical calculations were funded by RFBR and NSFC as the research project No. 19-54-53004 and RFBR research project No. 20-04-00085. The development of structural atomistic model of berovin without calcium ions generated by the I-TASSER server was funded by project 0721-2020-0033 of the Russian Ministry of Science and Education.
Аннотация: Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460-470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein-substrate complex was optimized using a linear scaling quantum-mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60 degrees of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified.
WOS
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova, Ludmila P., Lyakhovich, Maria S., Mineev, Konstantin S., Petushkov, Valentin N., Zagitova, Renata, I, Tsarkova, Aleksandra S., Kovalchuk, Sergey, I, Yampolsky, Ilia, V, Vysotski, Eugene S., Kaskova, Zinaida M.
Заглавие : Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation
Колич.характеристики :4 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-04-00085]; Russian Foundation for Basic Research, Krasnoyarsk Territory [20-44-242003]; Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds; Russian Science FoundationRussian Science Foundation (RSF) [17-1401169p]; Russian FederationRussian Federation [LS-2605.2020.4]
Место публикации : Org. Lett.: AMER CHEMICAL SOC, 2021. - Vol. 23, Is. 17. - С. 6846-6849. - ISSN 1523-7060, DOI 10.1021/acs.orglett.1c02410. - ISSN 1523-7052(eISSN)
Примечания : Cited References:20. - This work was supported by grant 20-04-00085 of the Russian Foundation for Basic Research, grant 20-44-242003 of the Russian Foundation for Basic Research, Krasnoyarsk Territory, and Krasnoyarsk Regional Fund of Science in part of purification and spectral characterization of native compounds, grant 17-1401169p of the Russian Science Foundation, and the President of Russian Federation grant for Leading Scientific Schools LS-2605.2020.4 in part of structural elucidation of native products and organic synthesis. We thank Konstantin Antonov (IBCh RAS) and Igor Ivanov (IBCh RAS) for the registration of HRMS spectra.
Предметные рубрики: CRYSTAL-STRUCTURE
BIOLUMINESCENCE
OBELIN
RESIDUES
BINDING
Аннотация: Ca2+-regulated photoproteins of ctenophores lose bioluminescence activity when exposed to visible light. Little is known about the chemical nature of chromophore photo-inactivation. Using a total synthesis strategy, we have established the structures of two unusual coelenterazine products, isolated from recombinant berovin of the ctenophore Beroe abyssicola, which are Z/E isomers. We propose that during light irradiation, these derivatives are formed from 2-hydroperoxycoelenterazine via the intermediate 8a-peroxide by a mechanism reminiscent of that previously described for the auto-oxidation of green-fluorescent-protein-like chromophores.
WOS
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena V., Bartsev, Sergey I., van Berkel, Willem J. H., Vysotski, Eugene S.
Заглавие : Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+-regulated Photoproteins of Different Organisms
Колич.характеристики :8 с
Коллективы : RFBR [14-04-31092]; Russian Academy of Sciences [01201351504, 01201351502]
Место публикации : Photochem. Photobiol.: WILEY, 2017. - Vol. 93, Is. 2. - С. 495-502. - ISSN 0031-8655, DOI 10.1111/php.12664. - ISSN 1751-1097(eISSN)
Примечания : Cited References:55. - This work was supported by RFBR grant 14-04-31092 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 01201351504 and 01201351502).
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
AEQUORIN BIOLUMINESCENCE
SEQUENCE-ANALYSIS
Аннотация: Upon binding their metal ion cofactors, Ca2+-regulated photoproteins display a rapid increase of light signal, which reaches its peak within milliseconds. In the present study, we investigate bioluminescence kinetics of the entire photoprotein family. All five recombinant hydromedusan Ca2+-regulated photoproteinsaequorin from Aequorea victoria, clytin from Clytia gregaria, mitrocomin from Mitrocoma cellularia and obelins from Obelia longissima and Obelia geniculatademonstrate the same bioluminescent kinetics pattern. Based on these findings, for the first time we propose a unanimous kinetic model describing the bioluminescence mechanism of Ca2+-regulated photoproteins.
WOS,
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Larionova, Marina D., Markova, Svetlana V., Vysotski, Eugene S.
Заглавие : Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa
Колич.характеристики :8 с
Коллективы : Russian Science Foundation [14-14-01119]
Место публикации : Photochem. Photobiol.: WILEY, 2017. - Vol. 93, Is. 2. - С. 503-510. - ISSN 0031-8655, DOI 10.1111/php.12694. - ISSN 1751-1097(eISSN)
Примечания : Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation.
Предметные 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.
WOS,
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena V., van Berkel, Willem J. H., Vysotski, Eugene S.
Заглавие : Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria
Колич.характеристики :10 с
Коллективы : Russian Science Foundation [14-14-01119]
Место публикации : FEBS Lett.: WILEY-BLACKWELL, 2016. - Vol. 590, Is. 3. - С. 307-316. - ISSN 0014-5793, DOI 10.1002/1873-3468.12052. - ISSN 1873-3468(eISSN)
Примечания : Cited References:34. - This study was supported by the grant 14-14-01119 of the Russian Science Foundation.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
ENERGY-TRANSFER
CA2+-REGULATED
Ключевые слова (''Своб.индексиров.''): 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.
WOS,
Scopus
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Natashin P..., Vysotski E..., Liu Z.J.
Заглавие : Three-dimensional structures of mutants of Ca2+-regulated photoprotein obelin provide insight into molecular mechanisms underlying changes in bioluminescent properties
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29. - С. 36-36. - ISSN 1522-7235. - ISSN 1522-7243
Примечания : Cited References: 2
WOS
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L.P., Markova S.V., Golz S..., Frank L.A., Vysotski E.S.
Заглавие : The recombinant Ca(2+)-regulated photoprotein berovin from Beroe abyssicola displays in vitro both luciferase and photoprotein activities
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2006. - Vol. 21, Is. 5. - С. 272-272. - ISSN 1522-7235
Примечания : Cited References: 0
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Natashin P.V., Vysotski E.S.
Заглавие : The photoprotein obelin as a bioluminescent reporter to monitor protein-protein interactions in vivo and in vitro by protein-fragment complementation assays
Колич.характеристики :1 с
Место публикации : J. Biotechnol.: ELSEVIER SCIENCE BV, 2010. - Vol. 150: 14th International Biotechnology Symposium and Exhibition (IBS-2008) (SEP 14-18, 2010, Rimini, ITALY). - С. S93-S93. - ISSN 0168-1656, DOI 10.1016/j.jbiotec.2010.08.241
Примечания : Cited References: 0
Ключевые слова (''Своб.индексиров.''): bioluminescence--reporter--obelin--protein-protein interactions
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17.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Vysotski E.S.
Заглавие : THE MAIN FUNCTION OF HIS175, TRP179, AND TYR190 RESIDUES OF THE OBELIN BINDING SITE IS TO STABILIZE THE HYDROPEROXYCOELENTERAZINE INTERMEDIATE
Колич.характеристики :4 с
Место публикации : BIOLUMINESCENCE AND CHEMILUMINESCENCE: CHEMISTRY, BIOLOGY AND APPLICATIONS: WORLD SCIENTIFIC PUBL CO PTE LTD, 2007. - 14th International Symposium on Bioluminescence and Chemiluminescence (OCT 15-19, 2006, San Diego, CA). - С. 7-10. - ISBN 978-981-270-816-8, DOI 10.1142/9789812770196_0002
Примечания : Cited References: 7
Предметные рубрики: PHOTOPROTEIN OBELIN
BIOLUMINESCENCE
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Burakova L.P., Golz S..., Malikova N.P., Frank L.A., Vysotski E.S.
Заглавие : The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein
Колич.характеристики :15 с
Место публикации : FEBS J.: WILEY-BLACKWELL, 2012. - Vol. 279, Is. 5. - С. 856-870. - ISSN 1742-464X, DOI 10.1111/j.1742-4658.2012.08476.x
Примечания : Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany).
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
C-TERMINAL PROLINE
SEQUENCE-ANALYSIS
MNEMIOPSIS-SP
COELENTERAZINE-BINDING
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
CRYSTAL-STRUCTURES
EXCITED-STATE
CDNA CLONING
Ключевые слова (''Своб.индексиров.''): bioluminescence--calcium--coelenterazine--luciferase--mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L.P., Markova S.V., Golz S..., Frank L.A., Vysotski E.S.
Заглавие : The isospecies of Ca(2+)-regulated photoprotein bolinopsin from Bolinopsis infundibulum
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2006. - Vol. 21, Is. 5. - С. 273-273. - ISSN 1522-7235
Примечания : Cited References: 0
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Westphal A.H., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : The intrinsic fluorescence of apo-obelin and apo-aequorin and use of its quenching to characterize coelenterazine binding
Колич.характеристики :6 с
Коллективы : Wageningen University Sandwich PhD-Fellowship Program [02.512.12. 2006]; Ministry of Education and Science of Russian Federation, MCB Program of RAS [1211.2008.4]; SB RAS
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2009. - Vol. 583, Is. 12. - С. 1939-1944. - ISSN 0014-5793, DOI 10.1016/j.febslet.2009.04.043
Примечания : Cited References: 28. - We thank Prof. John Lee for valuable suggestions and providing constructive criticisms. The work was supported by Wageningen University Sandwich PhD-Fellowship Program, Grants 02.512.12. 2006 and 1211.2008.4 of Ministry of Education and Science of Russian Federation, MCB Program of RAS, and by Grant No. 2 of SB RAS.
Предметные рубрики: CRYSTAL-STRUCTURE
CA2+-REGULATED PHOTOPROTEINS
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
W92F OBELIN
CALCIUM
REGENERATION
APOAEQUORIN
EXPRESSION
Ключевые слова (''Своб.индексиров.''): bioluminescence--photoprotein--trp fluorescence
Аннотация: The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2 +/- 0.12 mu M) and apo-obelin (0.2 +/- 0.04 mu M). Stopped-flow measurements of fluorescence quenching showed that coelenterazine binding is a millisecond-scale process, in contrast to the formation of an active photoprotein complex taking several hours. This finding evidently shows that the rate-limiting step of active photoprotein formation is the conversion of coelenterazine into its 2-hydroperoxy derivative. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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