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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva, Elena, V, Gulnov, Dmitry, V, Gerasimova, Marina A., Sukovatyi, Lev A., Burakova, Ludmila P., Karuzina, Natalya E., Melnik, Bogdan S., Kratasyuk, Valentina A.
Заглавие : Bacterial Luciferases from Vibrio harveyi and Photobacterium leiognathi Demonstrate Different Conformational Stability as Detected by Time-Resolved Fluorescence Spectroscopy
Колич.характеристики :17 с
Коллективы : 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)
Место публикации : Int. J. Mol. Sci.: MDPI, 2021. - Vol. 22, Is. 19. - Ст.10449. - ISSN 1422-0067(eISSN), DOI 10.3390/ijms221910449
Примечания : 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).
Предметные рубрики: TRYPTOPHAN FLUORESCENCE
CRYSTAL-STRUCTURE
SUBUNIT
BIOLUMINESCENCE
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./p
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tyulkova N.A., Sandalova T.P.
Заглавие : Comparative study of temperature effects on bacterial luciferases
Колич.характеристики :10 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1996. - Vol. 61, Is. 2. - P205-214. - ISSN 0006-2979
Примечания : Cited References: 23
Предметные рубрики: BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Maksimova E.E., Popova L.Y., Kargatova T.V., Shpagina V.V.
Заглавие : Controlled expression of bacterial luminescence genes cloned in a multicopy recombinant plasmid
Колич.характеристики :4 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1997. - Vol. 66, Is. 2. - P184-187. - ISSN 0026-2617
Примечания : Cited References: 17
Предметные рубрики: GENETICALLY-MODIFIED MICROORGANISMS
BIOLUMINESCENCE
ENVIRONMENT
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Liu Z.J., Markova S.S., Frank L.A., Lee J..., Vysotski E.S., Wang B.C.
Заглавие : Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 angstrom: Why it is not a calcium-regulated photoprotein
Колич.характеристики :6 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2008. - Vol. 7, Is. 4. - С. 442-447. - ISSN 1474-905X, DOI 10.1039/b716535h
Примечания : Cited References: 49
Предметные рубрики: HYDROID OBELIA-GENICULATA
AMINO-ACID-SEQUENCE
CA2+-REGULATED PHOTOPROTEINS
RENIFORMIS LUCIFERASE
ENERGY-TRANSFER
CDNA CLONING
BIOLUMINESCENCE
AEQUORIN
PURIFICATION
EXPRESSION
Аннотация: Bioluminescence in the sea pansy Renilla involves two distinct proteins, a Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP contains one tightly bound coelenterazine molecule, which becomes available for reaction with luciferase and O-2 only subsequent to Ca2+ binding. CBP belongs to the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand" Ca2+-binding sites. The overall spatial structure of recombinant selenomethionine-labeled CBP determined at 1.7 angstrom, is found to approximate the protein scaffold characteristic of the class of Ca2+-regulated photoproteins. Photoproteins however, catalyze molecular oxygen addition to coelenterazine producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the bioluminescence reaction. However in CBP this first step of oxygen addition is not allowed. The different amino acid environments and hydrogen bond interactions within the binding cavity are proposed to account for the different properties of the two classes of proteins.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J...
Заглавие : Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1
Колич.характеристики :6 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 25. - С. 8413-8418. - ISSN 0006-2960, DOI 10.1021/bi952691v
Примечания : Cited References: 24
Предметные рубрики: LUMAZINE PROTEIN
LUMINOUS BACTERIUM
STRAIN Y-1
BIOLUMINESCENCE
EMISSION
PURIFICATION
TRANSIENT
LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Medvedeva S. E., Artemenko K. S., Krivosheenko A. A., Rusinova A. G., Rodicheva E. K., Puzyr A. P., Bondar V. S.
Заглавие : Growth and light emission of luminous basidiomycetes cultivated on solid media and in submerged culture
Колич.характеристики :13 с
Коллективы : RF Government [11.G34.31.058]; SB RAS [71, 38]
Место публикации : Mycosphere: MYCOSPHERE PRESS, 2014. - Vol. 5, Is. 4. - С. 565-577. - ISSN 2077-7000, DOI 10.5943/mycosphere/5/4/9
Примечания : 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).
Предметные рубрики: MYCELIAL GROWTH
PANELLUS-STYPTICUS
BIOLUMINESCENCE
LUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Burakova L.P., Vysotski E.S.
Заглавие : High-active truncated luciferase of copepod Metridia longa
Колич.характеристики :6 с
Место публикации : Biochem. Biophys. Res. Commun.: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2012. - Vol. 417, Is. 1. - С. 98-103. - ISSN 0006-291X, DOI 10.1016/j.bbrc.2011.11.063
Примечания : 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.
Предметные рубрики: COELENTERAZINE-BINDING PROTEIN
REPORTER-GENE-EXPRESSION
RENILLA LUCIFERASE
GAUSSIA LUCIFERASE
LIGHT-EMITTER
IN-VIVO
BIOLUMINESCENCE
PHOTOPROTEINS
CDNA
SUBSTRATE
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Vysotski E.S.
Заглавие : Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase
Колич.характеристики :4 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2013. - Vol. 450, Is. 1. - С. 147-150. - ISSN 1607-6729, DOI 10.1134/S1607672913030095
Примечания : 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).
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
GENE-EXPRESSION
CDNA
CLONING
BIOLUMINESCENCE
RENIFORMIS
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : SANDALOVA T.P., TYULKOVA N.A.
Заглавие : INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE
Колич.характеристики :7 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 6. - P552-558. - ISSN 0006-2979
Примечания : Cited References: 21
Предметные рубрики: AMINO-ACID SEQUENCE
NUCLEOTIDE-SEQUENCE
REACTIVE SULFHYDRYL
PHOTOBACTERIUM-LEIOGNATHI
VIBRIO-HARVEYI
BIOLUMINESCENCE
SUBUNIT
REGION
GENE
Ключевые слова (''Своб.индексиров.''): 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.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Vysotski E.S., Westphal A.H., van Mierlo CPM, van Berkel WJH
Заглавие : Ligand binding and conformational states of the photoprotein obelin
Колич.характеристики :7 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2012. - Vol. 586, Is. 23. - С. 4173-4179. - ISSN 0014-5793, DOI 10.1016/j.febslet.2012.10.015
Примечания : 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.
Предметные рубрики: RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
LIGHT-EMISSION
APO-AEQUORIN
BIOLUMINESCENCE
COELENTERAZINE
LUMINESCENCE
STABILITY
ANGSTROM
PROTEINS
Ключевые слова (''Своб.индексиров.''): 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.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYDRYAKOVA G.A., KUZNETSOV A.M., PRIMAKOVA G.A., CHUGAEVA Y.V., FISH A.M.
Заглавие : LUMINESCENT BACTERIAL SYMBIONTS AND COMMENSALS OF LUMINESCENT AND NONLUMINESCENT MARINE ANIMALS OF THE INDIAN-OCEAN
Колич.характеристики :4 с
Место публикации : Microbiology: MAIK NAUKA/INTERPERIODICA, 1995. - Vol. 64, Is. 5. - P589-592. - ISSN 0026-2617
Примечания : Cited References: 18
Предметные 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.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Boyandin A..., Kalacheva G.S., Medvedeva S..., Rodicheva E..., Volova T.G.
Заглавие : Luminous bacteria as producers of polyhydroxyalkanoates
Место публикации : Macromol. Symp.: WILEY-V C H VERLAG GMBH, 2008. - Vol. 269: 4th European Symposium on Biopolymers (OCT 02-04, 2007, Kusadasi, TURKEY). - С. 17-22. - 6. - ISSN 1022-1360, DOI 10.1002/masy.200850904
Примечания : Cited References: 16
Предметные рубрики: VIBRIO-HARVEYI
BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Natashin P.V., Song L..., Zhou Y.G., van Berkel WJH, Liu Z.J., Vysotski E.S.
Заглавие : Oxygen Activation of Apo-obelin-Coelenterazine Complex
Колич.характеристики :7 с
Место публикации : ChemBioChem: WILEY-V C H VERLAG GMBH, 2013. - Vol. 14, Is. 6. - С. 739-745. - ISSN 1439-4227, DOI 10.1002/cbic.201300002
Примечания : 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.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
JELLYFISH CLYTIA-GREGARIA
CRYSTAL-STRUCTURE
CA2+-DISCHARGED PHOTOPROTEIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
MOLECULAR-OXYGEN
AEQUORIN
CALCIUM
BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarionov B.A., Frank L.A., Illarionova V.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator
Колич.характеристики :27 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - С. 223-249. - ISSN 0076-6879
Примечания : Cited References: 58
Предметные рубрики: PHOTOPROTEIN OBELIN
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
DIRECTED MUTAGENESIS
SEQUENCE-ANALYSIS
HYDROID OBELIA
AEQUORIN
PROTEIN
BIOLUMINESCENCE
LUMINESCENCE
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : 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.
Заглавие : SIMILARITIES AND DIFFERENCES BETWEEN THE CHAETOPTERUS VARIOPEDATUS POLYCHAETE LUCIFERASES DEPENDING ON THE TYPE OF HABITAT
Колич.характеристики :6 с
Место публикации : Bull. Russ. State Med. Univ.: PIROGOV RUSSIAN NATL RESEARCH MEDICAL UNIV, 2021. - Is. 5. - С. 41-46. - ISSN 2500-1094, DOI 10.24075/vrgmu.2021.049. - ISSN 2542-1204(eISSN)
Примечания : Cited References:20
Предметные рубрики: BIOLUMINESCENCE
ANNELIDA
SYSTEM
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.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : 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.
Заглавие : Stimulation of luminescence of mycelium of luminous fungus Neonothopanus nambi by ionizing radiation
Колич.характеристики :8 с
Коллективы : 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]
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29, Is. 7. - С. 703-710. - ISSN 1522-7235, DOI 10.1002/bio.2656. - ISSN 1522-7243
Примечания : 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).
Предметные рубрики: BIOLUMINESCENCE
COMPONENTS
MECHANISMS
SYSTEM
Ключевые слова (''Своб.индексиров.''): 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.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Liu Z.J., Vysotski E.S., Lee J..., Rose J.P., Wang B.C.
Заглавие : Structure based mechanism of the Ca2+ -induced release of coelenterazine from the Renilla binding protein
Колич.характеристики :11 с
Место публикации : Proteins: WILEY-BLACKWELL, 2009. - Vol. 74, Is. 3. - С. 583-593. - ISSN 0887-3585, DOI 10.1002/prot.22173
Примечания : Cited References: 26
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
CRYSTAL-STRUCTURES
RENIFORMIS
LUCIFERASE
BIOLUMINESCENCE
PURIFICATION
ANGSTROM
MUELLERI
Ключевые слова (''Своб.индексиров.''): bioluminescence--ef-hand--coelenteramider--luciferase--ca2+-binding protein
Аннотация: The crystal structure of the Ca2+-loaded coelenterazine binding protein from Renilla muelleri in its apo-state has been determined at resolution 1.8 angstrom. Although calcium binding hardly affects the compact scaffold and overall fold of the structure before calcium addition, there are easily discerned shifts in the residues that were interacting with the coelenterazine and a repositioning of helices, to expose a cavity to the external solvent. Altogether these changes offer a straightforward explanation for how following the addition of Ca2+, the coelenterazine could escape and become available for bioluminescence on Renilla luciferase. A docking computation supports the possibility of a luciferase-binding protein complex.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Krasitskaya, Vasilisa V., Goncharova, Natalia S., Biriukov, Vladislav V., Bashmakova, Eugenia E., Kabilov, Marsel R., Baykov, Ivan K., Sokolov, Aleksey E., Frank, Ludmila A.
Заглавие : The Ca2+-Regulated Photoprotein Obelin as a Tool for SELEX Monitoring and DNA Aptamer Affinity Evaluation
Колич.характеристики :6 с
Коллективы : Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [18-38-00531]
Место публикации : Photochem. Photobiol.: WILEY, 2020. - Article in press. - ISSN 0031-8655, DOI 10.1111/php.13274. - ISSN 1751-1097(eISSN)
Примечания : Cited References:25. - This work has been supported by the Russian Foundation for Basic Research (RFBR) under the grant no 18-38-00531.
Предметные 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.
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19.

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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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogil'naya, O. A., Ronzhin, N. O., Medvedeva, S. E., Bondar', V. S.
Заглавие : Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission
Колич.характеристики :6 с
Коллективы : Siberian Branch of the Russian Academy of Sciences [71]
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2015. - Vol. 51, Is. 4. - С. 419-424. - ISSN 0003-6838, DOI 10.1134/S0003683815040110. - ISSN 1573-8183(eISSN)
Примечания : 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.
Предметные рубрики: OXIDATIVE STRESS
SYSTEM
FUNGI
BIOLUMINESCENCE
LUMINESCENCE
Ключевые слова (''Своб.индексиров.''): 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.
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