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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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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 . - ISSN 1661-6596
Кл.слова (ненормированные):
Bacterial luciferase -- Conforma-tional stability -- FRET -- Molecular dynamics -- Time-resolved spectroscopy -- Tryptophan fluorescence -- Unfolding pathway -- Urea-induced denaturation
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 ?-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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Photobiology Laboratory, Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142290, Russian Federation

Доп.точки доступа:
Nemtseva, E. V.; Gulnov, D. V.; Gerasimova, M. A.; Sukovatyi, L. A.; Burakova, L. P.; Karuzina, N. E.; Melnik, B. S.; Kratasyuk, V. A.

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Bioluminescent method in studying the complex effect of sewage components / D. I. Stom [et al.] // Archives of Environmental Contamination and Toxicology. - 1992. - Vol. 22, Is. 2. - P203-208 . - ISSN 0090-4341
Кл.слова (ненормированные):
heavy metal -- phenol derivative -- quinone derivative -- article -- bacterium -- bioluminescence -- cell membrane -- nonhuman -- priority journal -- sludge -- ultrastructure -- Benzoquinones -- Catechin -- Hydroquinones -- Luminescent Measurements -- Metals -- Phenol -- Phenols -- Photobacterium -- Sewage -- Vibrio -- Water Pollutants, Chemical -- Bacteria (microorganisms)
Аннотация: The inhibition of bacterial luminescence has been used in testing industrial enterprises sewage. The toxicity of the sewage is less than the total toxicity of separate components due to neutralization of quinone products of polyphenol oxidation in the reactions with the other phenol components of sewage. Toxicity increase is due to their influence on the cell membrane. Studies of cell ultrastructure confirm this fact. The studied mechanism of the complex effect allowed a more accurate forecast of the ecological situation during the discharge of phenol compounds and metals. It also showed the necessity of taking into account the complex effect of sewage components on contaminant discharge into water reservoirs.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stom, D.I.; Geel, T.A.; Balayan, A.E.; Shachova, G.I.; Kuznetsov, A.M.; Medvedeva, S.E.

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Characteristics of enclogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fischeri NAD(P)H : FMN-oxidoreductase [Text] / E. V. Vetrova [et al.] // Luminescence. - 2005. - Vol. 20: 11th International Symposium on Luminescence Spectrometry - Detection Techniques in Biomedical and Environmental Analysis (MAY 05-08, 2004, Beijing, JAPAN), Is. 3. - P. 205-209, DOI 10.1002/bio.815. - Cited References: 22 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology
Рубрики:
FLAVODOXIN
   ANISOTROPY
   REDUCTASE
   DYNAMICS
   SYSTEM
Кл.слова (ненормированные):
bacterial bioluminescence -- flavin fluorescence
Аннотация: The bioluminescent bacterial enzyme system NAD(P)H:FMN-oxidoreductase-luciferase has been used as a test system for ecological monitoring. One of the modes to quench bioluminescence is the interaction of xenobiotics with the enzymes, which inhibit their activity. The use of endogenous flavin fluorescence for investigation of the interactions of non-fluorescent compounds with the bacterial luciferase from Photobacterium leiognathi and NAD(P)H:FMN-oxidoreductase from Vibrio fischeri has been proposed. Fluorescence spectroscopy methods have been used to study characteristics of endogenous flavin fluorescence (fluorophore lifetime, the rotational correlation time). The fluorescence anisotropy behaviour of FMN has been analysed and compared to that of the enzyme-bound flavin. The fluorescence characteristics of endogenous flavin of luciferase and NAD(P)H:FMN-oxidoreductase have been shown to be applicable in studying enzymes' interactions with non-fluorescent compounds. Copyright (c) 2005 John Wiley & Sons, Ltd.

WOS
Держатели документа:
RAS, SB, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Wageningen & Res Ctr, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vetrova, E.V.; Kudryasheva, N.S.; Visser, AJWG; van Hoek, A...

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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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Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1 [Text] / V. N. Petushkov, B. G. Gibson, J. . Lee // Biochemistry. - 1996. - Vol. 35, Is. 25. - P8413-8418, DOI 10.1021/bi952691v. - Cited References: 24 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
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.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOLEC BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J...

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Disposable luciferase-based microfluidic chip for rapid assay of water pollution / I. Denisov [et al.] // Lumin. - 2018. - Vol. 33, Is. 6. - P1054-1061, DOI 10.1002/bio.3508 . - ISSN 1522-7235
Кл.слова (ненормированные):
bioassay -- lab-on-a-chip -- luciferase -- microfluidics -- solvent bonding
Аннотация: In the present study, we demonstrate the use of a disposable luciferase-based microfluidic bioassay chip for environmental monitoring and methods for fabrication. The designed microfluidic system includes a chamber with immobilized enzymes of bioluminescent bacteria Photobacterium leiognathi and Vibrio fischeri and their substrates, which dissolve after the introduction of the water sample and thus activate bioluminescent reactions. Limits of detection for copper (II) sulfate, 1,3-dihydroxybenzene and 1,4-benzoquinone for the proposed microfluidic biosensor measured 3 ?M, 15 mM, and 2 ?M respectively, and these values are higher or close to the level of conventional environmental biosensors based on lyophilized bacteria. Approaches for entrapment of enzymes on poly(methyl methacrylate) (PMMA) plates using a gelatin scaffold and solvent bonding of PMMA chip plates under room temperature were suggested. The proposed microfluidic system may be used with some available luminometers and future portable luminescence readers. © 2018 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Denisov, I.; Lukyanenko, K.; Yakimov, A.; Kukhtevich, I.; Esimbekova, E.; Belobrov, P.

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Formation of structured communities by natural and transgenic naphthalene-degrading bacteria [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2005. - Vol. 41, Is. 1. - P. 63-68, DOI 10.1007/s10438-005-0012-x. - Cited References: 18 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
GENETICALLY-ENGINEERED MICROORGANISM
   POLYCYCLIC AROMATIC-HYDROCARBONS
   BIOFILM FORMATION
   DEGRADATION
Аннотация: This study concerns the formation of structured communities by monocultures and binary associations of Pseudomonas fluorescens transgenic strains and natural heterotrophic bacterial species in naphthalene-containing media with various osmotic pressures. It was shown that cells of P. fluorescens strain 5RL, harboring a recombinant construct in the chromosome, were more resistant to the combined action of the stress factors under study than P. fluorescens 82/pUTK21, harboring a recombinant construct within a plasmid. Natural P. fluorescens 1 strains, particularly Vibrio sp. 14, were more viable at high osmotic pressures and naphthalene concentrations. Experiments with the combined introduction of transgenic and natural bacterial strains at high osmotic pressures demonstrated the stable coexistence of bacterial associations in biofilms, independent of naphthalene concentration. Strains considered for introduction into the environment for bioremediation should be assessed with regard to their susceptibility to the combined effect of anthropogenic and natural stress factors. The design of bacterial associations for the same purpose should take into account the effect of factors important for their survival in polluted areas.

WOS
Держатели документа:
Russian Acad Sci, Siberian Div, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Mogil'naya, O.A.; Krivomazova, E.S.; Kargatova, T.V.; Lobova, T.I.; Popova, L.Y.

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GLUTAMATE SYNTHESIS CONTROL IN VIBRIO-HARVEYI [Text] / V. B. GUREVICH [et al.] // Microbiology. - 1986. - Vol. 55, Is. 1. - P. 66-68. - Cited References: 10 . - ISSN 0026-2617

РУБ Microbiology

WOS
Держатели документа:
ACAD SCI USSR,INST BIOPHYS,NOVOSIBIRSK,USSR
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
GUREVICH, V.B.; SVETLAKOV, A.V.; POPOVA, L.Y.; SHENDEROV, A.N.

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10.

Green-Fluorescent Protein from the Bioluminescent Jellyfish Clytia gregaria Is an Obligate Dimer and Does Not Form a Stable Complex with the Ca2+-Discharged Photoprotein Clytin [Text] / N. P. Malikova [et al.] // Biochemistry. - 2011. - Vol. 50, Is. 20. - P4232-4241, DOI 10.1021/bi101671p. - Cited References: 50. - This work was supported by NATO Collaborative Linkage Grant 979229, Grants SB RAS No. 2 and RFBR 08-04-92209, 09-04-12022, and 09-04-00172, the MCB program of the Russian Academy of Sciences, and Bayer AG. . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
VIBRIO-FISCHERI Y1
   ENERGY-TRANSFER
   CORRELATION SPECTROSCOPY
   BACTERIAL LUCIFERASE
   REFRACTIVE-INDEX
   PHOTOBACTERIUM-LEIOGNATHI
   POLARIZED FLUORESCENCE
   EXCITATION TRANSFER
   RECOMBINANT OBELIN
   LUMAZINE PROTEIN
Аннотация: Green-fluorescent protein (GFP) is the origin of the green bioluminescence color exhibited by several marine hydrozoans and anthozoans. The mechanism is believed to be Forster resonance energy transfer (FRET) within a luciferase GFP or photoprotein-GFP complex. As the effect is found in vitro at micromolar concentrations, for FRET to occur this complex must have an affinity in the micromolar range. We present here a fluorescence dynamics investigation of the recombinant bioluminescence proteins from the jellyfish Clytia gregaria, the photoprotein clytin in its Ca2+-discharged form that is highly fluorescent (lambda(max) = 506 nm) and its GFP (cgreGFP; lambda(max) = 500 nm). Ca2+-discharged clytin shows a predominant fluorescence lifetime of 5.7 ns, which is assigned to the final emitting state of the bioluminescence reaction product, coelenteramide anion, and a fluorescence anisotropy decay or rotational correlation time of 12 ns (20 degrees C), consistent with tight binding and rotation with the whole protein. A 34 ns correlation time combined with a translational diffusion constant and molecular brightness from fluorescence fluctuation spectroscopy all confirm that cgreGFP is an obligate dimer down to nanomolar concentrations. Within the dimer, the two chromophores have a coupled excited-state transition yielding fluorescence depolarization via FRET with a transfer correlation time of 0.5 ns. The 34 ns time of cgreGFP showed no change upon addition of a 1000-fold excess of Ca2+-discharged clytin, indicating no stable complexation below 0.2 mM. It is proposed that any bioluminescence FRET complex with micromolar affinity must be one formed transiently by the cgreGFP dimer with a short-lived (millisecond) intermediate in the clytin reaction pathway.

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Malikova, Natalia P.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
[Visser, Nina V.
van Hoek, Arie] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Visser, Nina V.
van Hoek, Arie
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Skakun, Victor V.] Belarusian State Univ, Dept Syst Anal, Minsk 220050, Byelarus
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Visser, N.V.; van Hoek, A...; Skakun, V.V.; Vysotski, E.S.; Lee, J...; Visser, AJWG

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11.

Growth and luminescence of luminous bacteria promoted by agents of microbial origin. / E. K. Rodicheva [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P293-299 . - ISSN 0884-3996
Кл.слова (ненормированные):
amino acid -- carbohydrate -- folic acid -- luciferase -- nitrogen -- riboflavin -- article -- biosynthesis -- culture medium -- electron microscopy -- growth, development and aging -- kinetics -- luminescence -- metabolism -- Photobacterium -- physiology -- time -- ultrastructure -- Vibrio -- Amino Acids -- Carbohydrates -- Culture Media -- Folic Acid -- Kinetics -- Luciferase -- Luminescence -- Microscopy, Electron -- Nitrogen -- Photobacterium -- Riboflavin -- Time Factors -- Vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodicheva, E.K.; Trubachev, I.N.; Medvedeva, S.E.; Egorova, O.I.; , U - Shitova LYu

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12.

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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13.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive [Text] / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931. - Cited References: 41 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
BACTERIAL LUCIFERASE
   LUMAZINE PROTEIN
   FLAVIN INTERMEDIATE
   ANGSTROM RESOLUTION
   RIBOFLAVIN PROTEIN
   PURIFICATION
   MECHANISM
   EMISSION
   ALDEHYDE
   INHIBITION
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects call be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, when the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on-off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme, These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found or the protein-protein interaction in the absence of the aliphatic component.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M...; Gibson, B.G.; Lee, J...

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14.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- anisotropy -- antenna -- article -- bioluminescence -- complex formation -- energy transfer -- enzyme active site -- enzyme kinetics -- nonhuman -- priority journal -- protein protein interaction -- spectroscopy -- vibrionaceae -- Bacterial Proteins -- Carrier Proteins -- Cloning, Molecular -- Dithionite -- Flavin Mononucleotide -- Kinetics -- Luciferases -- Luminescent Measurements -- Luminescent Proteins -- Models, Structural -- Photobacterium -- Protein Binding -- Protein Conformation -- Recombinant Proteins -- Spectrophotometry -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Photobacterium leiognathi -- Vibrio fischeri -- Vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.

Scopus
Держатели документа:
Department of Biochemistry, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Acad. of Sci. of Russia, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M.; Gibson, B.G.; Lee, J.

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15.

Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes / B. A. Illarrionov [et al.] // Gene. - 1990. - Vol. 86, Is. 1. - P89-94 . - ISSN 0378-1119
Кл.слова (ненормированные):
Bioluminescence -- expression in E. coli -- luciferase -- molecular evolution -- nucleotide sequence -- protein alignment -- recombinant DNA -- luciferase -- amino acid sequence -- article -- bioluminescence -- fungus -- gene structure -- genetic engineering -- heredity -- nonhuman -- nucleotide sequence -- priority journal -- vibrionaceae -- Acyltransferases -- Amino Acid Sequence -- Bacterial Proteins -- Base Sequence -- Cloning, Molecular -- DNA, Bacterial -- Genes, Structural, Bacterial -- Luciferase -- Luminescence -- Molecular Sequence Data -- Operon -- Photobacterium -- Restriction Mapping -- Escherichia coli -- Fungi -- Photobacterium leiognathi -- Vibrio harveyi -- Vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, 660062, Russian Federation
All-Union Research Institute of Molecular Biology, Novosibirsk Region, 633159, Russian Federation
Institute of Biophysics, Krasnoyarsk, 660036, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, 630090, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarrionov, B.A.; Blinov, V.M.; Douchenko, A.P.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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16.

Kinetic analysis of bacterial water-organic media [Text] / I. E. Sukovataya, N. A. Tyulkova // Luminescence. - 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P. 271-273, DOI 10.1002/bio.649.abs. - Cited References: 10 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bacterial luciferase -- organic solvents -- Michaelis constant
Аннотация: The interaction of luciferases from two types of luminous bacteria, Photobacterium leiognathi and Vibrio harveyi, with their substrates [the photorecovered. FMNH2 and long-chain aldehydes-decanal (C-10), dodecanal (C-12) and tetradecanal (C-14)] in water-organic media was analysed using kinetic graphical methods. Moderate concentrations of organic solvents have been demonstrated to activate the bioluminescence, while higher concentrations inhibit it. The interactions of these effectors with luciferases show different types of kinetics, which depend on concentrations of solvents, kinds of enzymes and substrates. The apparent value of the Michaelis constant, K-m for C-14 of both luciferases and for C-10 of luciferase V. harveyi is enhanced with increasing concentration of the organic solvent, but K-m for C-12 and C-10 of luciferase P. leiognathi decreases. Obviously, at the specific binding of aldehydes with luciferases in the first case, hydrophobic interactions are realized, but in second, the electrostatic interactions are realized. The series of changes in parameters of bioluminescence reaction catalysed by different luciferases is obviously determined by their structural peculiarities. Copyright (C) 2001 John Wiley & Sons, Ltd.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sukovataya, I.E.; Tyulkova, N.A.

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17.

Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another / N. S. Rodionova, V. N. Petushkov, P. I. Belobrov // Biophysics. - 1988. - Vol. 33, Is. 3. - P424-430 . - ISSN 0006-3509
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, U.S.S.R. Academy of Sciences, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodionova, N.S.; Petushkov, V.N.; Belobrov, P.I.

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18.

Location of lectin exhibiting specificity for N-acetyl-D-galactosamine in cells of the symbiotic marine bacteria Photobacterium phosphoreum [Text] / G. A. Vydryakova, V. S. Bondar // Dokl. Biochem. Biophys. - 2008. - Vol. 420, Is. 1. - P155-157, DOI 10.1134/S1607672908030150. - Cited References: 14 . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VIBRIO-FISCHERI
   EUPRYMNA-SCOLOPES
   LIGHT ORGAN
   COLONIZATION

Держатели документа:
[Vydryakova, G. A.
Bondar, V. S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vydryakova, G.A.; Bondar, V.S.

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19.

LUMINESCENT PLANKTON BACTERIA FROM THE CORAL REEFS AND LITTORAL WATERS OF THE TROPICAL REGIONS OF THE INDIAN-OCEAN AND THE SOUTH CHINA SEA [Text] / G. A. PRIMAKOVA, A. M. KUZNETSOV // Microbiology. - 1990. - Vol. 59, Is. 5. - P. 630-637. - Cited References: 19 . - ISSN 0026-2617

РУБ Microbiology
Рубрики:
LUMINOUS BACTERIA
   SPECIES COMPOSITION
   MEDITERRANEAN SEA
   ESTUARY
   GULF
   ELAT
Аннотация: Luminescent bacteria were regularly encountered on the coral reefs of both the Indian Ocean and the South China Sea. Their counts in these regions amounted to 10(2) to 10(4) colony-forming units (CFU)/liter, and their proportion of the total numbers of saprophytic bacteria was 0.1-6.0%. Up to 85% of the luminescent bacteria occurred in the sea water in the form of aggregates ranging in size from 3-8-mu-m, to below 200-mu-m. The predominant species amongst the luminescent bacteria of these regions was Vibrio harvevi, comprising [4], with only 8.8% represented by Photobacterium leiognathi.

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

Доп.точки доступа:
PRIMAKOVA, G.A.; KUZNETSOV, A.M.

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20.

Luminous bacteria as potential producers of resorbed polyhydroxyalkanoate polyesters [Text] / A. N. Boyandin [et al.] // Dokl. Biochem. Biophys. - 2007. - Vol. 416, Is. 01.06.2013. - P248-251, DOI 10.1134/S1607672907050067. - Cited References: 15 . - 4. - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
VIBRIO-HARVEYI

Держатели документа:
[Boyandin, A. N.
Kalacheva, G. S.
Rodicheva, E. K.
Volova, T. G.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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