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1.


   
    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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2.


   
    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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3.


   
    Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria [Text] / V. N. Petrushkov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P. 164-180. - Cited References: 18 . - ISSN 0076-6879
РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
YELLOW FLUORESCENT PROTEIN
   FISCHERI STRAIN Y-1

   AMINO-ACID-SEQUENCE

   VIBRIO-FISCHERI

   PHOTOBACTERIUM-LEIOGNATHI

   RIBOFLAVIN PROTEIN

   LUMINOUS BACTERIUM

   LUMAZINE PROTEIN

   FMN

   Y1


WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Agr Univ Wageningen, Dept Biochem, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petrushkov, V.N.; Gibson, B.G.; Visser, AJWG; Lee, J...

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4.


   
    Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria [Text] / V. N. Petushkov [et al.] // J. Phys. Chem. B. - 2003. - Vol. 107, Is. 39. - P. 10934-10939, DOI 10.1021/jp034266e. - Cited References: 52 . - ISSN 1520-6106
РУБ Chemistry, Physical
Рубрики:
TIME-RESOLVED FLUORESCENCE
   VIBRIO-FISCHERI Y1

   FEMTOSECOND SOLVATION DYNAMICS

   FLAVIN ADENINE-DINUCLEOTIDE

   PHOTOBACTERIUM-LEIOGNATHI

   BIOLOGICAL WATER

   SOLVENT DYNAMICS

   DIELECTRIC-RELAXATION

   MOLECULAR-DYNAMICS

   TRYPTOPHAN

Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by similar to7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

WOS
Держатели документа:
Univ Wageningen & Res Ctr, Biochem & Biophys Lab, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
Vrije Univ Amsterdam, Fac Sci & Engn, Dept Phys & Astron, NL-1081 HV Amsterdam, Netherlands
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Vrije Univ Amsterdam, Fac Earth & Life Sci, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; van Stokkum, IHM; Gobets, B...; van Mourik, F...; Lee, J...; van Grondelle, R...; Visser, AJWG

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5.


   
    Effect of low-dose ionizing radiation on luminous marine bacteria: radiation hormesis and toxicity [Text] / N. S. Kudryasheva, T. V. Rozhko // J. Environ. Radioact. - 2015. - Vol. 142. - P68-77, DOI 10.1016/j.jenvrad.2015.01.012. - Cited References:131. - This work was supported by the Russian Foundation for Basic Research, Grant No.13-04-01305a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. The part of the work (review of effects of americium-241) was supported by the Russian Science Foundation, Grant No. 14-14-00076. . - ISSN 0265-931X. - ISSN 1879-1700
РУБ Environmental Sciences
Рубрики:
RECOMBINANT LUMINESCENT MICROORGANISMS
   PHOTOBACTERIUM-LEIOGNATHI

Кл.слова (ненормированные):
Marine bacteria -- Low-dose effects -- Radiation hormesis -- Radiotoxicity -- Reactive oxygen species
Аннотация: The paper summarizes studies of effects of alpha- and beta-emitting radionuclides (americium-241, uranium-235+238, and tritium) on marine microorganisms under conditions of chronic low-dose irradiation in aqueous media. Luminous marine bacteria were chosen as an example of these microorganisms; bioluminescent intensity was used as a tested physiological parameter. Non-linear dose-effect dependence was demonstrated. Three successive stages in the bioluminescent response to americium-241 and tritium were found: 1 - absence of effects (stress recognition), 2 - activation (adaptive response), and 3 - inhibition (suppression of physiological function, i.e. radiation toxicity). The effects were attributed to radiation hormesis phenomenon. Biological role of reactive oxygen species, secondary products of the radioactive decay, is discussed. The study suggests an approach to evaluation of non-toxic and toxic stages under conditions of chronic radioactive exposure. (C) 2015 Elsevier Ltd. All rights reserved.

WOS
Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
Siberian Fed Univ, Krasnoyarsk 660041, Russia
Krasnoyarsk State Med Acad, Krasnoyarsk 660022, Russia

Доп.точки доступа:
Kudryasheva, N. S.; Rozhko, T. V.; Russian Foundation for Basic Research [13-04-01305a]; Program "Molecular and Cellular Biology" of the Russian Academy of Sciences [VI 57.1.1]; Russian Science Foundation [14-14-00076]

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