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Stimulation of luminescence of mycelium of luminous fungus Neonothopanus nambi by ionizing radiation [Text] / T. V. Kobzeva [et al.] // Luminescence. - 2014. - Vol. 29, Is. 7. - P703-710, DOI 10.1002/bio.2656. - Cited References: 29. - The work was supported by the Program of Siberian Branch of Russian Academy of Sciences (project no. 71), Council for Grants of the President of the Russian Federation for Support of Leading Scientific Schools (project no. NSh 2272.2012.3), the Russian Foundation for Basic Research (project no. 12-03-33082), and the Program of Government of Russian Federation "On the Efforts for Attracting Leading Researchers to Educational Institutions of Russia" (grant no. 11.G34.31.0058). . - ISSN 1522-7235. - ISSN 1522-7243

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENCE
   COMPONENTS
   MECHANISMS
   SYSTEM
Кл.слова (ненормированные):
Higher luminous fungi -- Neonothopanus nambi -- ionizing irradiation -- reactive oxygen species -- lipid peroxidation
Аннотация: The luminescent system of higher luminous fungi is not fully understood and the enzyme/substrate pair of the light emission reaction has not been isolated. It was suggested that luminescence of fungi involves oxidase-type enzymes, and reactive oxygen species are important for fungal light production. Generation of reactive oxygen species can be stimulated by ionizing irradiation, which has not been studied for luminous fungi. We report the effect of X-irradiation on the luminescence of fungus Neonothopanus nambi. Experiments were performed withmyceliumon a home-built setup based on an X-ray tube and monochromator/photomultiplier tube. Application of X-rays does not change the emission spectrum, but after approximately 20 min of continuous irradiation, light production from unsupported mycelium starts growing and increases up to approximately five times. After peaking, its level decreases irrespective of the presence of X-irradiation. After staying at a certain level, light production collapses to zero, which is not related to the drying of the mycelium or thermal impact of radiation. The observed shape of kinetics is characteristic of a multistage and/or chain reaction. The time profile of light production must reflect the current levels of radicals present in the system and/or the activity of enzyme complexes involved in light production. Copyright (C) 2014 John Wiley & Sons, Ltd.

WOS
Держатели документа:
[Kobzeva, Tatiana V.
Melnikov, Anatoly R.
Karogodina, Tatiana Y.
Zikirin, Samat B.
Stass, Dmitri V.
Molin, Yuri N.] Inst Chem Kinet & Combust SB RAS, Novosibirsk 630090, Russia
[Melnikov, Anatoly R.
Zikirin, Samat B.
Stass, Dmitri V.] Novosibirsk State Univ, Novosibirsk 630090, Russia
[Rodicheva, Emma K.
Medvedeva, Svetlana E.
Puzyr, Alexey P.
Bondar, Vladimir S.
Gitelson, Joseph I.] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
[Rodicheva, Emma K.
Medvedeva, Svetlana E.
Puzyr, Alexey P.
Burov, Andrey A.
Bondar, Vladimir S.
Gitelson, Joseph I.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Burov, Andrey A.] Special Design Technol Bur Nauka SB RAS, Krasnoyarsk 660049, Russia
ИБФ СО РАН
СКТБ : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kobzeva, T.V.; Melnikov, A.R.; Karogodina, T.Y.; Zikirin, S.B.; Stass, D.V.; Molin, Y.N.; Rodicheva, E.K.; Medvedeva, S.E.; Puzyr, A.P.; Burov, A.A.; Bondar, V.S.; Gitelson, J.I.; Program of Siberian Branch of Russian Academy of Sciences [71]; Council for Grants of the President of the Russian Federation for Support of Leading Scientific Schools [NSh 2272.2012.3]; Russian Foundation for Basic Research [12-03-33082]; Program of Government of Russian Federation "On the Efforts for Attracting Leading Researchers to Educational Institutions of Russia" [11.G34.31.0058]

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Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2015. - Vol. 51, Is. 4. - P419-424, DOI 10.1134/S0003683815040110. - Cited References:35. - The authors are grateful to N. V. Psurtseva (curator of the collection of basidiomycetes of the Botanical Institute, Russian Academy of Science) for help with the species affiliation of the IBSO 2328 culture. This work was supported by the Program of Interdisciplinary Projects of the Siberian Branch of the Russian Academy of Sciences, project no. 71. . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
OXIDATIVE STRESS
   SYSTEM
   FUNGI
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
basidiomycetes -- luminescence -- peroxidase -- catalase
Аннотация: The peroxidase and catalase activities in the mycelium of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in normal conditions and under stress were compared. An increase in the luminescence level was observed under stress, as well as an increase in peroxidase and catalase activities. Moreover, the peroxidase activity in extracts of A. borealis mycelium was found to be almost one and a half orders of magnitude lower, and the catalase activity more than two orders of magnitude higher in comparison with the N. nambi mycelium. It can be suggested that the difference between the brightly luminescent and dimly luminescent mycelium of N. nambi is due to the content of (HO2)-O-2 or other peroxide compounds.

WOS,
Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogil'naya, O. A.; Ronzhin, N. O.; Medvedeva, S. E.; Bondar', V. S.; Siberian Branch of the Russian Academy of Sciences [71]

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Growth and light emission of luminous basidiomycetes cultivated on solid media and in submerged culture [Text] / S. E. Medvedeva [et al.] // Mycosphere. - 2014. - Vol. 5, Is. 4. - P565-577, DOI 10.5943/mycosphere/5/4/9. - Cited References:23. - This study was supported by grant No. 11.G34.31.058 (RF Government) and Projects No. 71 and No. 38 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
MYCELIAL GROWTH
   PANELLUS-STYPTICUS
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
luminescence -- luminous higher fungi -- mycelium
Аннотация: There are higher fungi that emit visible light; however, little is known about their requirements for good growth and bright luminescence. Knowledge of these requirements is extremely important for maintaining fungal cultures in laboratory conditions and preparation of luminous mycelia for research purposes. Luminous higher fungi Panellus stipticus, Armillaria sp. and Neonothopanus nambi isolated from different climatic areas and maintained in CCIBSO 836 (Collection of IBP SB RAS, Russia) were used for experiments. Techniques for static and submerged cultivation of mycelia of higher fungi have been developed and optimized for the production of samples of aerial and globular mycelia with prolonged and stable luminescence. We investigated the growth characteristics and luminescence of mycelia cultivated in/on different nutrient media, and the effects of deionized water and mechanical damage on the light emission of mycelia. An increase in luminescence intensity of fungal mycelia can be obtained during cultivation of fungi on a nutrient medium with a certain composition. A significant increase in light emission from N. nambi mycelium can also be obtained after its incubation in water and mechanical damage. The light emission from N. nambi mycelium was greatly enhanced after these treatments, in contrast to the mycelia of Armillaria sp. or P. stipticus. Cultivation conditions that enable growing mycelia with high levels of luminescence will expedite further studies to gain a better understanding of fungal bioluminescence.

WOS
Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Medvedeva, S. E.; Artemenko, K. S.; Krivosheenko, A. A.; Rusinova, A. G.; Rodicheva, E. K.; Puzyr, A. P.; Bondar, V. S.; RF Government [11.G34.31.058]; SB RAS [71, 38]

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LUMINESCENT BACTERIAL SYMBIONTS AND COMMENSALS OF LUMINESCENT AND NONLUMINESCENT MARINE ANIMALS OF THE INDIAN-OCEAN [Text] / G. A. VYDRYAKOVA [et al.] // Microbiology. - 1995. - Vol. 64, Is. 5. - P. 589-592. - Cited References: 18 . - ISSN 0026-2617

РУБ Microbiology
Рубрики:
BIOLUMINESCENCE
SEAWATER
Аннотация: Approximately 100 fish belonging to 24 families and several representatives of cephalopods, prawns, and euphausiids were investigated for the presence of luminescent bacteria. Species identification of isolated luminescent bacteria was performed, and the frequency and ratio of their occurrence in the gastrointestinal microflora of marine animals were determined. Luminescent bacteria occurred in 23 - 65% of the fish, depending on the habitat depth, and their ratio varied from 8 to 60% of the total gastrointestinal microflora of fish. The free-living luminescent bacteria were found in 50% of the seawater samples from depths down to 1000 m. The luminescent bacterium Photobacterium phosphoreum was dominant among the isolated cultures.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
VYDRYAKOVA, G.A.; KUZNETSOV, A.M.; PRIMAKOVA, G.A.; CHUGAEVA, Y.V.; FISH, A.M.

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Comparative study of temperature effects on bacterial luciferases [Text] / N. A. Tyulkova, T. P. Sandalova // Biochem.-Moscow. - 1996. - Vol. 61, Is. 2. - P. 205-214. - Cited References: 23 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- temperature -- activation energy
Аннотация: Effects of temperature on bioluminescent patterns of luciferases from luminescent bacteria Vibrio harveyi, Vibrio fischeri, Photobacterium leiognathi, and Photobacterium phosphoreum were studied. The highest luminescence level was observed at 15-25 degrees C for the luciferase from P. phosphoreum, at 20-30 degrees C for the V. fischeri and P. leiognathi enzymes, and at 30-37 degrees C for the enzyme from V. harveyi. All the luciferases were significantly stabilized at increased salt concentrations, at low pH values, or in the presence of dithiothreitol (DTT) and EDTA. The addition of DTT and EDTA affected the reversible stage of enzyme inactivation, while salts reduced the rate of the irreversible stage. A peak corresponding to aggregated protein was detected by gel chromatography of irreversibly inactivated luciferase. Activation energies were calculated for each luciferase in bioluminescent reactions with decanal, dodecanal, tetradecanal, and without aldehydes. The activation energy of the reaction with tetradecanal was much lower than those with the other aldehydes. The temperature dependence of the lifetime of the long-lived reaction intermediate showed that in the 10-30 degrees C interval all the luciferases, except for the enzyme from V. harveyi, have only one active form.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tyulkova, N.A.; Sandalova, T.P.

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Controlled expression of bacterial luminescence genes cloned in a multicopy recombinant plasmid [Text] / E. E. Maksimova [et al.] // Microbiology. - 1997. - Vol. 66, Is. 2. - P. 184-187. - Cited References: 17 . - ISSN 0026-2617

РУБ Microbiology
Рубрики:
GENETICALLY-MODIFIED MICROORGANISMS
BIOLUMINESCENCE
ENVIRONMENT
Кл.слова (ненормированные):
recombinant plasmid -- Escherichia coli -- luminescence -- catabolite repression
Аннотация: Luminescence and growth responses of the recombinant strain Escherichia coil Z905 (Ap(r)Lux(+)) to different concentrations of ampicillin depended on the source of carbon and energy. When glycerol was used as the substrate, the intensity of luminescence rose with the ampicillin concentration in the medium. Glucose caused catabolite repression of cell luminescence up to the late stationary phase, and ampicillin enhanced this effect. The feasibility of controlling the expression of cloned lux genes was shown.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Maksimova, E.E.; Popova, L.Y.; Kargatova, T.V.; Shpagina, V.V.

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Unexpected Coelenterazine Degradation Products of Beroe abyssicola Photoprotein Photoinactivation / L. P. Burakova, M. S. Lyakhovich, K. S. Mineev [et al.] // Org. Lett. - 2021. - Vol. 23, Is. 17. - P6846-6849, DOI 10.1021/acs.orglett.1c02410. - 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. . - ISSN 1523-7060. - ISSN 1523-7052

РУБ Chemistry, Organic
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
Держатели документа:
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photo Biol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.

Доп.точки доступа:
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.; Mineev, Konstantin; Tsarkova, Aleksandra; Vysotski, Eugene; Kaskova, Zinaida; Burakova, Lyudmila; 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]

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Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy / E. V. Nemtseva, D. V. Gulnov, M. A. Gerasimova [et al.] // Int. J. Mol. Sci. - 2021. - Vol. 22, Is. 19. - Ст. 10449, DOI 10.3390/ijms221910449. - Cited References:45. - The research was partially funded by the Ministry of Science and Higher Education of the Russian Federation (projects No. FSRZ-2020-0006); by the RFBR and Krasnoyarsk Territory and Krasnoyarsk Regional Fund of Science (projects No. 20-44-243002 and 20-44-240006); and by the RFBR (project No. 20-34-90118). . - ISSN 1422-0067

РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
TRYPTOPHAN FLUORESCENCE
   CRYSTAL-STRUCTURE
   SUBUNIT
   BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- urea-induced denaturation -- time-resolved -- spectroscopy -- conformational stability -- FRET -- tryptophan fluorescence -- molecular dynamics -- unfolding pathway
Аннотация: Detecting the folding/unfolding pathways of biological macromolecules is one of the urgent problems of molecular biophysics. The unfolding of bacterial luciferase from Vibrio harveyi is well-studied, unlike that of Photobacterium leiognathi, despite the fact that both of them are actively used as a reporter system. The aim of this study was to compare the conformational transitions of these luciferases from two different protein subfamilies during equilibrium unfolding with urea. Intrinsic steady-state and time-resolved fluorescence spectra and circular dichroism spectra were used to determine the stages of the protein unfolding. Molecular dynamics methods were applied to find the differences in the surroundings of tryptophans in both luciferases. We found that the unfolding pathway is the same for the studied luciferases. However, the results obtained indicate more stable tertiary and secondary structures of P. leiognathi luciferase as compared to enzyme from V. harveyi during the last stage of denaturation, including the unfolding of individual subunits. The distinctions in fluorescence of the two proteins are associated with differences in the structure of the C-terminal domain of alpha-subunits, which causes different quenching of tryptophan emissions. The time-resolved fluorescence technique proved to be a more effective method for studying protein unfolding than steady-state methods.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino 142290, Russia.

Доп.точки доступа:
Nemtseva, Elena, V; Gulnov, Dmitry, V; Gerasimova, Marina A.; Sukovatyi, Lev A.; Burakova, Ludmila P.; Karuzina, Natalya E.; Melnik, Bogdan S.; Kratasyuk, Valentina A.; Burakova, Lyudmila; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; RFBRRussian Foundation for Basic Research (RFBR) [20-34-90118]; Krasnoyarsk Regional Fund of Science [20-44-243002, 20-44-240006]; RFBRRussian Foundation for Basic Research (RFBR)

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SIMILARITIES AND DIFFERENCES BETWEEN THE CHAETOPTERUS VARIOPEDATUS POLYCHAETE LUCIFERASES DEPENDING ON THE TYPE OF HABITAT / K. V. Purtov, V. N. Petushkov, N. S. Rodionova [et al.] // Bull. Russ. State Med. Univ. - 2021. - Is. 5. - P41-46, DOI 10.24075/vrgmu.2021.049. - Cited References:20 . - ISSN 2500-1094. - ISSN 2542-1204

РУБ Medicine, General & Internal
Рубрики:
BIOLUMINESCENCE
ANNELIDA
SYSTEM
Кл.слова (ненормированные):
bioluminescence -- luciferase -- polychaetes -- Chaetopterus variopedatus -- marine worms
Аннотация: The marine polychaete Chaetopterus variopedatus (Renier) (family Chaetopteridae) is a cosmopolitan species complex, consisting of distinct populations/subspecies. The worms release glowing (460 nm) clouds of mucus when disturbed, and their parapodia often glow brightly. Currently, it is still unclear how exactly the bioluminescence system of these polychaetes functions. It has been previously assumed that the C. variopedatus luciferase may be used for detection of ferroptosis, the recently explored pathway of programmed cell death, resulting from accumulation of the ferrous ions. This study was aimed to extract and characterize the C. variopedatus luciferases, as well as to compare luciferases obtained from C. variopedatus of different populations. When extracting the enzyme responsible for bioluminescence from the frozen samples of Brazilian C. variopedatus using the improved method, two active luciferases, L1 and L2, were obtained. We assumed that one of the listed above luciferases was responsible for luminescence of the mucus and the other luciferase was responsible for luminescence in parapodia, and used the method for the distinct samples of mucus and parapodia of the living Far Eastern C. variopedatus. However, mucus of the latter turned out to be non-glowing. It is shown that luciferase L2 is responsible for luminescence in the parapodia of the C. variopedatus polychaete, since this luciferase has been found in the total biomass of Brazilian polychaetes and parapodia of Far Eastern polychaetes. Luminescence of the Brazilian C. variopedatus mucus is attributed to the functioning of luciferase L1, which is lacking in the mucus of the Far Eastern subspecies. The range of luciferase isoforms in polychaetes C. variopedatus depends on the place of origin.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Krasnoyarsk Sci Ctr, Siberian Branch, Moscow, Russia.
Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow, Russia.
Pacific State Med Univ, Vladivostok, Russia.
Pirogov Russian Natl Res Med Univ, Moscow, Russia.

Доп.точки доступа:
Purtov, K., V; Petushkov, V. N.; Rodionova, N. S.; Chepurnykh, T., V; Kozhemyako, V. B.; Zagitova, R., I; Shcheglov, A. S.; Ziganshin, R. H.; Tsarkova, A. S.

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10.

^a343.17.09^2VINITI
Б 26

Барцев, С. И.
К вопросу о временной организации бактериальной люминесценции [Текст] : научное издание / С. И. Барцев, И. И. Гительзон // Stud. biophys. - 1985. - Т. 105, N 3. - С. 149-156 . - ISSN 0081-6337

ГРНТИ

34.17.09

РУБ 343.17.09
Рубрики:
БИОЛЮМИНЕСЦЕНЦИЯ
   МЕХАНИЗМЫ
   МАТЕМАТИЧЕСКИЕ МОДЕЛИ
   БАКТЕРИИ
   BACTERIAS
   BIOLUMINESCENCE
   MATHEMATICAL MODELS

Доп.точки доступа:
Гительзон, И.И.

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11.

^a343.17.09.11^2VINITI
Г 51

Гительзон, И. И.
Перспективы применения биолюминесцентных методов в медицине [Текст] : научное издание / И. И. Гительзон, Т. П. Сандалова // Вестн. АМН СССР. - 1990. - N 9. - С. 31-35 . - ISSN 0002-3027

ГРНТИ

34.17.09

РУБ 343.17.09.11
Рубрики:
БИОЛЮМИНЕСЦЕНЦИЯ
   ПРИМЕНЕНИЕ
   МЕДИЦИНА
   BIOLUMINESCENCE
   APPLICATION IN MEDICINE

Доп.точки доступа:
Сандалова, Т.П.

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12.

The Ca2+-Regulated Photoprotein Obelin as a Tool for SELEX Monitoring and DNA Aptamer Affinity Evaluation / V. V. Krasitskaya, N. S. Goncharova, V. V. Biriukov [et al.] // Photochem. Photobiol. - 2020, DOI 10.1111/php.13274. - Cited References:25. - This work has been supported by the Russian Foundation for Basic Research (RFBR) under the grant no 18-38-00531. . - Article in press. - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CARDIAC TROPONIN-I
   BIOLUMINESCENCE
   IMMUNOASSAY
   APTASENSOR
   DIAGNOSIS
Аннотация: Bioluminescent solid-phase analysis was proposed to monitor the selection process and to determine binding characteristics of the aptamer-target complexes during design and development of the specific aptamers. The assay involves Ca2+-regulated photoprotein obelin as a simple, sensitive and fast reporter. Applicability and the prospects of the approach were exemplified by identification of DNA aptamers to cardiac troponin I, a highly specific early biomarker for acute myocardial infarction. Two structurally different aptamers specific to various epitopes of troponin I were obtained and then tested in a model bioluminescent assay.

WOS
Держатели документа:
Fed Res Ctr KSC SB RAS, Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Inst Chem Biol & Fundamental Med SB RAS, Novosibirsk, Russia.
Fed Res Ctr KSC SB RAS, Kirensky Inst Phys, Krasnoyarsk, Russia.

Доп.точки доступа:
Krasitskaya, Vasilisa V.; Goncharova, Natalia S.; Biriukov, Vladislav V.; Bashmakova, Eugenia E.; Kabilov, Marsel R.; Baykov, Ivan K.; Sokolov, Aleksey E.; Frank, Ludmila A.; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]

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13.

INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE [Text] / T. P. SANDALOVA, N. A. TYULKOVA // Biochem.-Moscow. - 1992. - Vol. 57, Is. 6. - P. 552-558. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   REACTIVE SULFHYDRYL
   PHOTOBACTERIUM-LEIOGNATHI
   VIBRIO-HARVEYI
   BIOLUMINESCENCE
   SUBUNIT
   REGION
   GENE
Кл.слова (ненормированные):
LUCIFERASE -- N-ETHYLMALEIMIDE
Аннотация: The kinetics of inactivation of luciferases from four species of luminescent bacteria by the thiol reagent N-ethylmaleimide were investigated The dependencies of inactivation on ionic strength differed among the enzymes. Increasing the molarity of the buffer increased the rate of inactivation of all luciferases except that of Vibrio harveyi. Modification of Photobacterium phosphoreum luciferase decreased the maximal intensity of bioluminescence, whereas modification of Photobacterium leiognathi and Vibrio fischeri luciferases in high ionic strength buffers decreased the maximal intensity of bioluminescence and changed the luminescence decay rate constant. High ionic strength apparently alters the conformational states of the luciferases.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
SANDALOVA, T.P.; TYULKOVA, N.A.

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14.

Oxygen Activation of Apo-obelin-Coelenterazine Complex / E. V. Eremeeva [et al.] // ChemBioChem. - 2013. - Vol. 14, Is. 6. - P739-745, DOI 10.1002/cbic.201300002. - Cited References: 46. - The work was supported by grants from the RFBR 12-04-91153, and NSFC 31270795 and 31021062, by the Russian Federation Government Program "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of the Russian Federation "Leading Science School" (grant 1044.2012.2). E.V.E. was supported by a Wageningen University Sandwich PhD Fellowship Program. . - ISSN 1439-4227

РУБ Biochemistry & Molecular Biology + Chemistry, Medicinal
Рубрики:
GREEN-FLUORESCENT PROTEIN
   JELLYFISH CLYTIA-GREGARIA
   CRYSTAL-STRUCTURE
   CA2+-DISCHARGED PHOTOPROTEIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MOLECULAR-OXYGEN
   AEQUORIN
   CALCIUM
   BIOLUMINESCENCE
Кл.слова (ненормированные):
aequorin -- coelenterazine -- luminescence -- photoprotein -- protein folding
Аннотация: Ca2+-regulated photoproteins use a noncovalently bound 2-hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo-obelincoelenterazine complex and the kinetics of its conversion into active photoprotein after exposure to air. Our studies suggest that coelenterazine bound within the anaerobic complex might be a mixture of N7-protonated and C2() anionic forms, and that oxygen shifts the equilibrium in favor of the C2() anion as a result of peroxy anion formation. Proton removal from N7 and further protonation of peroxy anion and the resulting formation of 2-hydroperoxycoelenterazine in obelin might occur with the assistance of His175. It is proposed that this conserved His residue might play a key role both in formation of active photoprotein and in Ca2+-triggering of the bioluminescence reaction.

Держатели документа:
[Eremeeva, Elena V.
Natashin, Pavel V.
Liu, Zhi-Jie] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Siberian Fed Univ, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
[Eremeeva, Elena V.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Song, Lei
Zhou, Yuguang] Chinese Acad Sci, China Gen Microbiol Culture Collect Ctr, Inst Microbiol, Beijing 100101, Peoples R China
[Liu, Zhi-Jie] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Natashin, P.V.; Song, L...; Zhou, Y.G.; van Berkel, WJH; Liu, Z.J.; Vysotski, E.S.

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15.

Ligand binding and conformational states of the photoprotein obelin / E. V. Eremeeva [et al.] // FEBS Lett. - 2012. - Vol. 586, Is. 23. - P4173-4179, DOI 10.1016/j.febslet.2012.10.015. - Cited References: 24. - The work was supported by RFBR grant 12-04-00131, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.058), by the Program "Molecular and Cellular Biology" of RAS. The Wageningen University Sandwich PhD-Fellowship Program supported E.V.E. . - ISSN 0014-5793

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE
   LIGHT-EMISSION
   APO-AEQUORIN
   BIOLUMINESCENCE
   COELENTERAZINE
   LUMINESCENCE
   STABILITY
   ANGSTROM
   PROTEINS
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Thermostability
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Westphal, Adrie H.
van Mierlo, Carlo P. M.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Vysotski, Eugene S.] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Vysotski, E.S.; Westphal, A.H.; van Mierlo, CPM; van Berkel, WJH

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16.

High-active truncated luciferase of copepod Metridia longa / S. V. Markova, L. P. Burakova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 2012. - Vol. 417, Is. 1. - P98-103, DOI 10.1016/j.bbrc.2011.11.063. - Cited References: 31. - This study was supported by the Grants 16.512.11.2141 and 64987.2010.4 of the Ministry of Education and Science of Russian Federation. . - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
COELENTERAZINE-BINDING PROTEIN
   REPORTER-GENE-EXPRESSION
   RENILLA LUCIFERASE
   GAUSSIA LUCIFERASE
   LIGHT-EMITTER
   IN-VIVO
   BIOLUMINESCENCE
   PHOTOPROTEINS
   CDNA
   SUBSTRATE
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Mammalian expression -- Secretion
Аннотация: The technology of real-time imaging in living cells is crucial for understanding of intracellular events. For this purpose, bioluminescent reporters have been introduced as sensitive and convenient tools. Metridia luciferase (MLuc) from the copepod Metridia longa is a coelenterazine-dependent luciferase containing a natural signal peptide for secretion. We report the high-active MLuc mutants with deletion of the N-terminal variable part of amino acid sequence. The MLuc variants were produced in Escherichia coil cells, converted to an active protein, and characterized. We demonstrate that the truncated MLucs have significantly increased bioluminescent activity as against the wild type enzyme but substantially retain other properties. One of the truncated variants of MLuc was transiently expressed in HEK 293 cells. The results clearly suggest that the truncated Metridia luciferase is well suited as a secreted reporter ensuring higher detection sensitivity in comparison with a wild type enzyme. (C) 2011 Elsevier Inc. All rights reserved.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
Siberian Fed Univ, Dept Biophys, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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17.

^a314.23.27.07.11^2VINITI
В 93

Высоцкий, Е. С.
Выделение и очистка Ca-зависимого фотопротеина - обелина из гидроидных полипов Obelia longissima [Текст] : научное издание / Е. С. Высоцкий, В. С. Бондарь, В. Н. Летунов // Биохимия. - 1989. - Т. 54, N 6. - С. 965-973 . - ISSN 0320-9725

ГРНТИ

31.23.27

РУБ 314.23.27.07.11
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
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Летунов, В.Н.

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18.

Luminous bacteria as producers of polyhydroxyalkanoates [Text] / A. . Boyandin [et al.] // Macromol. Symp. - 2008. - Vol. 269: 4th European Symposium on Biopolymers (OCT 02-04, 2007, Kusadasi, TURKEY). - P17-22, DOI 10.1002/masy.200850904. - Cited References: 16 . - 6. - ISSN 1022-1360

РУБ Polymer Science
Рубрики:
VIBRIO-HARVEYI
BIOLUMINESCENCE
Кл.слова (ненормированные):
luminous bacteria -- polyhydroxyalkanoates -- polyhydroxybutyrate
Аннотация: The study addresses the ability of luminous bacteria of different taxa (Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio harveyi, Vibrio fischeri) to synthesize polyesters of hydrocarbon acids (polyhydroxyalkanoates, PHAs) as storage macromolecules. The screened strains widely varied in their PHA productivity. Conditions for attaining high polymer yields (including two- and three-component polymers) in batch culture have been determined. The attained polymer yields reached 40-70% of dry cell biomass. The results suggest a conclusion that luminous microorganisms can be considered as producers of multi-component PHAs.

Держатели документа:
[Boyandin, Anatoly
Kalacheva, Galina S.
Medvedeva, Svetlana
Rodicheva, Emma
Volova, Tatiana G.] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
[Volova, Tatiana G.] Siberian Fed Univ, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A...; Kalacheva, G.S.; Medvedeva, S...; Rodicheva, E...; Volova, T.G.

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19.

Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase / E. V. Eremeeva, S. V. Markova, E. S. Vysotski // Dokl. Biochem. Biophys. - 2013. - Vol. 450, Is. 1. - P147-150, DOI 10.1134/S1607672913030095. - Cited References: 14. - This work was supported by the Ministry of Education and Science of the Russian Federation (Government Contract no. 16.512.11.2141) and Council of the President of the Russian Federation on Grants and State Support of Leading Scientific Schools (project no. NSh-64987.2010.4). . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
   GENE-EXPRESSION
   CDNA
   CLONING
   BIOLUMINESCENCE
   RENIFORMIS

Scopus
Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodnyi pr. 79, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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20.

Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator [Text] / B. A. Illarionov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P223-249. - Cited References: 58 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
PHOTOPROTEIN OBELIN
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   DIRECTED MUTAGENESIS
   SEQUENCE-ANALYSIS
   HYDROID OBELIA
   AEQUORIN
   PROTEIN
   BIOLUMINESCENCE
   LUMINESCENCE

Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Univ Washington, Friday Harbor Labs, Friday Harbor, WA 98250 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarionov, B.A.; Frank, L.A.; Illarionova, V.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.

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