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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin
Колич.характеристики :9 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2013. - Vol. 12, Is. 6. - С. 1016-1024. - ISSN 1474-905X, DOI 10.1039/c3pp00002h
Примечания : Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
CA2+-BINDING PHOTOPROTEIN
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
MNEMIOPSIS-LEIDYI
LIGHT-EMISSION
W92F OBELIN
CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Lee J...
Заглавие : Ca2+-regulated photoproteins: Structural insight into the bioluminescence mechanism
Колич.характеристики :11 с
Место публикации : Accounts Chem. Res.: AMER CHEMICAL SOC, 2004. - Vol. 37, Is. 6. - С. 405-415. - ISSN 0001-4842, DOI 10.1021/ar0400037
Примечания : Cited References: 44
Предметные рубрики: AEQUORIN BIOLUMINESCENCE
SEQUENCE-ANALYSIS
CALCIUM-BINDING
CA2+-BINDING PHOTOPROTEIN
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
FUNCTIONAL PART
EXCITED-STATES
W92F OBELIN
COELENTERAZINE
Аннотация: The bioluminescent jellyfish has contributed two famous proteins to modern science: green fluorescent protein or GFP, which finds wide use as a probe in cell biology studies, and aequorin, which has been used for intracellular calcium measurement for more than 30 years. More recently, obelin, a protein from the bioluminescent hydroid and also in the family of what are called "Ca2+-regulated photoproteins", has been shown to have very attractive properties both in general applications and for basic structural biology investigations. This review will survey the new information into their molecular mechanism of bioluminescence action.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Malikova N.P., Burakova L.P., Markova S.V., Vysotski E.S.
Заглавие : Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration
Колич.характеристики :12 с
Коллективы : RFBR [12-04-00131]; Government of the Russian Federation [11.G34.31.0058]; Russian Academy of Sciences; Russian Federation "Leading Science School" [3951.2012.4]
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2014. - Vol. 406, Is. 23. - С. 5715-5726. - ISSN 1618-2642, DOI 10.1007/s00216-014-7986-2. - ISSN 1618-2650
Примечания : Cited References: 67. - This work was supported by RFBR grant 12-04-00131, by the programs of the Government of the Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) and "Molecular and Cellular Biology" of the Russian Academy of Sciences, and the grant from the President of the Russian Federation "Leading Science School" (3951.2012.4).
Предметные рубрики: LIGHT-SENSITIVE PHOTOPROTEIN
CTENOPHORE BEROE ABYSSICOLA
GREEN-FLUORESCENT PROTEIN
INTRACELLULAR CALCIUM
SEQUENCE-ANALYSIS
CA-2+-ACTIVATED PHOTOPROTEIN
CA2+-BINDING PHOTOPROTEIN
SEMISYNTHETIC AEQUORINS
LUMINESCENT PROTEIN
RECOMBINANT OBELIN
Ключевые слова (''Своб.индексиров.''): calcium--coelenterazine--aequorin--obelin--clytin--mitrocomin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y(2) receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., van Berkel WJH, Vysotski E.S.
Заглавие : Role of key residues of obelin in coelenterazine binding and conversion into 2-hydroperoxy adduct
Колич.характеристики :7 с
Коллективы : RFBR [12-04-00131]; Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" [11.G34.31.0058]; "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" [3951.2012.4]; Wageningen University Sandwich PhD-Fellowship Program
Место публикации : J. Photochem. Photobiol. B-Biol.: ELSEVIER SCIENCE SA, 2013. - Vol. 127. - С. 133-139. - ISSN 1011-1344, DOI 10.1016/j.jphotobiol.2013.08.012
Примечания : Cited References: 65. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 3951.2012.4). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
APO-OBELIN
CA2+-BINDING PHOTOPROTEIN
VIOLET BIOLUMINESCENCE
AEQUORIN REGENERATION
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
MNEMIOPSIS-LEIDYI
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--obelin--aequorin--photoprotein
Аннотация: Bioluminescence of a variety of marine organisms is caused by monomeric Ca2+-regulated photoproteins, to which a peroxy-substituted coelenterazine, 2-hydroperoxycoelenterazine, is firmly bound. From the spatial structure the side chains of Tyr138, His175, Trp179, and Tyr190 of obelin are situated within the substrate-binding pocket at hydrogen bond distances with different atoms of the 2-hydroperoxycoelenterazine. Here we characterized several obelin mutants with substitutions of these residues regarding their bioluminescence, coelenterazine binding, and kinetics of active obelin formation. We demonstrate that Tyr138, His175, Trp179, and Tyr190 are all important for coelenterazine activation; substitution of any of these residues leads to significant decrease of the apparent reaction rate. The hydrogen bond network formed by Tyr138, Trp179 and Tyr190 participates in the proper positioning of coelenterazine in the active site and subsequent stabilization of the 2-hydroperoxy adduct of coelenterazine. His175 might serve as a proton shuttle during 2-hydroperoxycoelenterazine formation. (C) 2013 Elsevier B.V. All rights reserved.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Vysotski E.S., Chen C.J., Rose J.P., Lee J..., Wang B.C.
Заглавие : Structure of the Ca2+-regulated photoprotein obelin at 1.7 angstrom resolution determined directly from its sulfur substructure
Колич.характеристики :9 с
Место публикации : Protein Sci.: CAMBRIDGE UNIV PRESS, 2000. - Vol. 9, Is. 11. - С. 2085-2093. - ISSN 0961-8368
Примечания : Cited References: 41
Предметные рубрики: CALCIUM-MODULATED PROTEINS
AMINO-ACID SEQUENCE
CA-2+-BINDING PHOTOPROTEIN
CA2+-BINDING PHOTOPROTEIN
MACROMOLECULAR STRUCTURES
3-DIMENSIONAL STRUCTURE
ANOMALOUS SCATTERING
CRYSTAL-STRUCTURES
DIFFRACTION DATA
BINDING SITE
Ключевые слова (''Своб.индексиров.''): bioluminescence--crystallography--obelin--photoprotein--single wavelength anomalous scattering--solvent flattening--sulfur phasing
Аннотация: The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 Angstrom resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Natashin P.V., Ding W..., Eremeeva E.V., Markova S.V., Lee J..., Vysotski E.S., Liu Z.J.
Заглавие : Structures of the Ca2+-regulated photoprotein obelin Y138F mutant before and after bioluminescence support the catalytic function of a water molecule in the reaction
Колич.характеристики :13 с
Коллективы : RFBR [12-04-91153, 12-04-00131, 14-04-31092]; Chinese Academy of Sciences; NSFC; Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' [11.G34.31.0058]; RAS; Russian Federation 'Leading Science School' [3951.2012.4]
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: WILEY-BLACKWELL, 2014. - Vol. 70. - С. 720-732. - ISSN 0907-4449, DOI 10.1107/S1399004713032434. - ISSN 1399-0047
Примечания : Cited References: 71. - We acknowledge the use of beamline BL17U1 at the Shanghai Synchrotron Radiation Facility, China. This work was supported by RFBR grants 12-04-91153, 12-04-00131 and the China-Russia International Collaboration grant from the Chinese Academy of Sciences and NSFC, by the Programs of the Government of the Russian Federation 'Measures to Attract Leading Scientists to Russian Educational Institutions' (grant 11.G34.31.0058) and 'Molecular and Cellular Biology' of the RAS, the President of the Russian Federation 'Leading Science School' (grant 3951.2012.4). PVN and EVE were supported by RFBR grant 14-04-31092.
Предметные рубрики: AEQUORIN BIOLUMINESCENCE
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
CA2+-BINDING PHOTOPROTEIN
VIOLET BIOLUMINESCENCE
CALCIUM CONCENTRATION
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
MNEMIOPSIS-LEIDYI
EXCITED-STATES
Аннотация: Ca2+-regulated photoproteins, which are responsible for light emission in a variety of marine coelenterates, are a highly valuable tool for measuring Ca2+ inside living cells. All of the photoproteins are a single-chain polypeptide to which a 2-hydroperoxycoelenterazine molecule is tightly but noncovalently bound. Bioluminescence results from the oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. Here, the crystal structures of the Y138F obelin mutant before and after bioluminescence are reported at 1.72 and 1.30 angstrom resolution, respectively. The comparison of the spatial structures of the conformational states of Y138F obelin with those of wild-type obelin gives clear evidence that the substitution of Tyr by Phe does not affect the overall structure of both Y138F obelin and its product following Ca2+ discharge compared with the corresponding conformational states of wild-type obelin. Despite the similarity of the overall structures and internal cavities of Y138F and wild-type obelins, there is a substantial difference: in the cavity of Y138F obelin a water molecule corresponding to W2 in wild-type obelin is not found. However, in Ca2+-discharged Y138F obelin this water molecule now appears in the same location. This finding, together with the observed much slower kinetics of Y138F obelin, clearly supports the hypothesis that the function of a water molecule in this location is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion before its decomposition into the excited-state product. Although obelin differs from other hydromedusan Ca2+-regulated photoproteins in some of its properties, they are believed to share a common mechanism.
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