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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Titushin M.S., Feng Y.G., Lee J..., Vysotski E.S., Liu Z.J.
Заглавие : Protein-protein complexation in bioluminescence
Колич.характеристики :16 с
Место публикации : Protein Cell: HIGHER EDUCATION PRESS, 2011. - Vol. 2, Is. 12. - С. 957-972. - ISSN 1674-800X, DOI 10.1007/s13238-011-1118-y
Примечания : Cited References: 114. - The work was funded by "Fellowship for Young International Scientists" of Chinese Academy of Sciences. This work was supported by the National Natural Science Foundation of China (Grant Nos: 30870483, 31070660, 31021062 and 81072449), Ministry of Science and Technology of China (Nos. 2009DFB30310, 2009CB918803 and 2011CB911103), CAS Research Grants (Nos. YZ200839 and KSCX2-EW-J-3).
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
LUCIFERIN-BINDING-PROTEIN
RENILLA-RENIFORMIS LUCIFERASE
VIBRIO-FISCHERI Y1
JELLYFISH CLYTIA-GREGARIA
ALPHA/BETA-HYDROLASE FOLD
AMINO-ACID-SEQUENCE
BACTERIAL LUCIFERASE
ENERGY-TRANSFER
CRYSTAL-STRUCTURE
Ключевые слова (''Своб.индексиров.''): green-fluorescent protein (gfp)--photoprotein--luciferase--lumazine protein--forster resonance energy transfer (fret)--docking
Аннотация: In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca2+-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of X-ray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Visser N.V., van Hoek A..., Skakun V.V., Vysotski E.S., Lee J..., Visser AJWG
Заглавие : 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
Колич.характеристики :10 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2011. - Vol. 50, Is. 20. - С. 4232-4241. - ISSN 0006-2960, DOI 10.1021/bi101671p
Примечания : 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.
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Burakova L.P., Frank L.A., Golz S..., Korostileva K.A., Vysotski E.S.
Заглавие : Green-fluorescent protein from the bioluminescent jellyfish Clytia gregaria: cDNA cloning, expression, and characterization of novel recombinant protein
Колич.характеристики :9 с
Коллективы :
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2010. - Vol. 9, Is. 6. - С. 757-765. - ISSN 1474-905X, DOI 10.1039/c0pp00023j
Примечания : Cited References: 42. - We thank Dr John Lee (University of Georgia) for constructive suggestions. This work was supported by the Russian Foundation for Basic Research (Grants: 08-04-92209 and 09-04-12022), "Molecular and Cell Biology" program of RAS, and Bayer AG (Germany).
Предметные рубрики: ENERGY-TRANSFER
CA2+-REGULATED PHOTOPROTEINS
RENILLA BIOLUMINESCENCE
ANGSTROM RESOLUTION
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
EXCITED-STATE
AEQUORIN
PURIFICATION
OBELIN
Аннотация: The bioluminescent systems of many marine organisms are comprised of two proteins - the Ca2+-regulated photoprotein and green-fluorescent protein (GFP). This work reports the cloning of the full-size cDNA encoding GFP (cgreGFP) from jellyfish Clytia gregaria, its expression and properties of the recombinant protein. The overall degree of identity between the amino acid sequence of the novel cgreGFP and the sequence of GFP (avGFP) from Aequorea victoria is 42% (similarity - 64%) despite these GFPs originating from jellyfish that both belong to the same class, Hydrozoa. However although the degree of identity is low, three residues, Ser-Tyr-Gly, which form the chromophore are identical in both GFPs. The cgreGFP displayed two absorption peaks at 278 and 485 nm, and the fluorescence maximum at 500 nm. The fluorescence quantum yield was determined to be 0.86, the brightness to be 54 mM(-1) cm(-1). For the first time we have also demonstrated an efficient radiationless energy transfer in vitro between clytin and cgreGFP in solution at micromolar concentrations. The cgreGFP may be a useful intracellular fluorescent marker, as it was able to be expressed in mammalian cells.
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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) : Titushin M.S., Markova S.V., Frank L.A., Malikova N.P., Stepanyuk G.A., Lee J..., Vysotski E.S.
Заглавие : Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase
Колич.характеристики :8 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2008. - Vol. 7, Is. 2. - С. 189-196. - ISSN 1474-905X, DOI 10.1039/b713109g
Примечания : Cited References: 41
Предметные рубрики: CRYSTAL-STRUCTURE
LIGHT-EMISSION
CA2+-REGULATED PHOTOPROTEINS
BIOLUMINESCENT REPORTER
RENIFORMIS LUCIFERASE
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
ENERGY-TRANSFER
EXCITED-STATE
CALCIUM
Аннотация: The Renilla bioluminescent system in vivo is comprised of three proteins-the luciferase, green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called luciferin-binding protein (LBP). This work reports the cloning of the full-size cDNA encoding CBP from soft coral Renilla muelleri, its overexpression and properties of the recombinant protein. The apo-CBP was quantitatively converted to CBP by simple incubation with coelenterazine. The physicochemical properties of this recombinant CBP are determined to be practically the same as those reported for the CBP (LBP) of R. reniformis. CBP is a member of the four-EF-hand Ca2+-binding superfamily of proteins with only three of the EF-hand loops having the Ca2+-binding consensus sequences. There is weak sequence homology with the Ca2+-regulated photoproteins but only as a result of the necessary Ca2+-binding loop structure. In combination with Renilla luciferase, addition of only one Ca2+ is sufficient to release the coelenterazine as a substrate for the luciferase for bioluminescence. This combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone as the substrate for luciferase. This increased quantum yield, a difference of bioluminescence spectra, and markedly different kinetics, implicate that a CBP-luciferase complex might be involved.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Burakova L.P., Krasitskaya V.V., Kudryavtsev A.N., Shimomura O..., Frank L.A.
Заглавие : Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules
Колич.характеристики :7 с
Коллективы : RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2014. - Vol. 13, Is. 3. - С. 541-547. - ISSN 1474-905X, DOI 10.1039/c3pp50369k. - ISSN 1474-9092
Примечания : Cited References: 22. - The work was supported by RFBR grant 12-04-00753-a, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058).
Предметные рубрики: GREEN FLUORESCENT PROTEIN
CA2+-REGULATED PHOTOPROTEIN
BIOLUMINESCENT IMMUNOASSAY
COELENTERAZINE BINDING
ANGSTROM RESOLUTION
ENERGY-TRANSFER
FUSION PROTEIN
APO-OBELIN
AEQUORIN
EXPRESSION
Аннотация: Previous studies have stated that aequorin loses most of its bioluminescence activity upon modification of the C-terminus, thus limiting the production of photoprotein fusion proteins at its N-terminus. In the present work, we investigate the importance of the C-terminal proline and the hydrogen bonds it forms for photoprotein active complex formation, stability and functional activity. According to the crystal structures of obelin and aequorin, two Ca2+-regulated photoproteins, the carboxyl group of the C-terminal Pro forms two hydrogen bonds with the side chain of Arg21 (Arg15 in aequorin case) situated in the first a-helix. Whereas, deletion or substitution of the C-terminal proline could noticeably change the bioluminescence activity, stability or the yield of an active photoprotein complex. Therefore, modifications of the first alpha-helix Arg has a clear destructive effect on the main photoprotein properties. A C-terminal hydrogen-bond network is proposed to be important for the stability of photoprotein molecules towards external disturbances, when taking part in the formation of locked protein conformations and isolation of coelenterazine-binding cavities.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva, Elena V., van Berkel, Willem J. H., Vysotski, Eugene S.
Заглавие : Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria
Колич.характеристики :10 с
Коллективы : Russian Science Foundation [14-14-01119]
Место публикации : FEBS Lett.: WILEY-BLACKWELL, 2016. - Vol. 590, Is. 3. - С. 307-316. - ISSN 0014-5793, DOI 10.1002/1873-3468.12052. - ISSN 1873-3468(eISSN)
Примечания : Cited References:34. - This study was supported by the grant 14-14-01119 of the Russian Science Foundation.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
ENERGY-TRANSFER
CA2+-REGULATED
Ключевые слова (''Своб.индексиров.''): aequorin--bioluminescence--coelenterazine--fret--obelin--protein-protein--interaction
Аннотация: Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.
WOS,
Scopus
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