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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L..., Natashin P..., Markova S..., Eremeeva E..., Vysotsky E...
Заглавие : The C-terminal tyrosine deletion in mitrocomin increases its bioluminescent activity
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29. - С. 84-84. - ISSN 1522-7235. - ISSN 1522-7243
Примечания : Cited References: 6
Предметные рубрики: PHOTOPROTEIN
EXPRESSION
AEQUORIN
CLONING
CDNA
WOS
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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.
wos
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Natashin P.V., Markova S.V., Lee J., Vysotski E.S., Liu Z.-J.
Заглавие : Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins
Место публикации : FEBS J. - 2014. - Vol. 281, Is. 5. - С. 1432-1445. - ISSN 17424658 (ISSN) , DOI 10.1111/febs.12715
Ключевые слова (''Своб.индексиров.''): aequorin--bioluminescence--coelenterazine, obelin--6 (4 hydroxyphenyl) derivative--aequorin--benzene derivative--calcium ion--hydromedusan--mutant protein--obelin--oxygen--photoprotein--unclassified drug--amino acid substitution--article--bioluminescence--calcium transport--crystal structure--fluorescence--hydrogen bond--priority journal--protein conformation--protein structure--wild type--coelenterata--aequorin--bioluminescence--ca2+-regulated photoprotein--coelenterazine, obelin--amino acid substitution--animals--conserved sequence--crystallography, x-ray--hydrogen bonding--hydrozoa--luminescent proteins--models, molecular--mutagenesis, site-directed--mutant proteins--protein conformation--spectrophotometry
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2- hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Comparison of spatial structures and the hydrogen bond network formed into the substrate-binding cavity of WT obelin, F88Y obelin, and aequorin clearly shows that the main cause determining different light emission colors of hydromedusan photoproteins is a different arrangement of the hydrogen-bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine due to the presence of either Phe or Tyr residue. © 2014 FEBS.
Scopus
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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 Ca2+concentration
Место публикации :. - 2014. - ISSN 16182642 (ISSN) , DOI 10.1007/s00216-014-7986-2
Ключевые слова (''Своб.индексиров.''): aequorin--calcium--clytin--coelenterazine--mitrocomin--obelin
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 P2Y2 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. [Figure not available: see fulltext.] © 2014 Springer-Verlag Berlin Heidelberg.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gealageas R..., Malikova N.P., Picaud S..., Borgdorff A.J., Burakova L.P., Brulet P..., Vysotski E.S., Dodd R.H.
Заглавие : Bioluminescent properties of obelin and aequorin with novel coelenterazine analogues
Колич.характеристики :13 с
Коллективы : ICSN; CNRS Physics, Chemistry and Biology interface grant; RFBR [12-04-00131]; Government of Russian Federation [11.G34.31.0058]; ANR
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2014. - Vol. 406, Is. 11. - С. 2695-2707. - ISSN 1618-2642, DOI 10.1007/s00216-014-7656-4. - ISSN 1618-2650
Примечания : Cited References: 57. - R.G. acknowledges the ICSN for a fellowship. We are grateful for the ANR grant to P.B. and a CNRS Physics, Chemistry and Biology interface grant to R.H.D. and P.B.; N.P.M, L.P.B., and E.S.V. acknowledge the RFBR grant 12-04-00131 and the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant 11.G34.31.0058). P.B. and A.J.B. are indebted to Eric Karplus from Science Wares Inc. for helping with single-photon imaging software.
Предметные рубрики: PHOTOPROTEIN OBELIN
CRYSTAL-STRUCTURE
CA2+-REGULATED PHOTOPROTEINS
CA2+-ACTIVATED PHOTOPROTEIN
SEMISYNTHETIC AEQUORINS
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
BINDING PROTEIN
CALCIUM-BINDING
CA2+ DYNAMICS
Ключевые слова (''Своб.индексиров.''): bioluminescence--luciferase--photoprotein--coelenterazine
Аннотация: The main analytical use of Ca2+-regulated photoproteins from luminous coelenterates is for real-time non-invasive visualization of intracellular calcium concentration ([Ca2+](i)) dynamics in cells and whole organisms. A limitation of this approach for in vivo deep tissue imaging is the fact that blue light emitted by the photoprotein is highly absorbed by tissue. Seven novel coelenterazine analogues were synthesized and their effects on the bioluminescent properties of recombinant obelin from Obelia longissima and aequorin from Aequorea victoria were evaluated. Only analogues having electron-donating groups (m-OCH3 and m-OH) on the C6 phenol moiety or an extended resonance system at the C8 position (1-naphthyl and alpha-styryl analogues) showed a significant red shift of light emission. Of these, only the alpha-styryl analogue displayed a sufficiently high light intensity to allow eventual tissue penetration. The possible suitability of this compound for in vivo assays was corroborated by studies with aequorin which allowed the monitoring of [Ca2+](i) dynamics in cultured CHO cells and in hippocampal brain slices. Thus, the alpha-styryl coelenterazine analogue might be potentially useful for non-invasive, in vivo bioluminescence imaging in deep tissues of small animals.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Berestovskaya N.G., Shaloiko L.A., Gorokhovatsky A.Y., Bondar V.S., Vysotski E.S., Maximov J.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC, 1999. - Vol. 268, Is. 1. - P72-78. - ISSN 0003-2697, DOI 10.1006/abio.1998.3051
Примечания : Cited References: 22
Предметные рубрики: SEQUENCE-ANALYSIS
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
LIGHT-EMISSION
AEQUORIN
CDNA
CLONING
EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A., Petunin A.I., Vysotski E.S.
Заглавие : Conjugates of the Ca2+-regulated photoprotein obelin with immunoglobulins: Synthesis and use as labels in bioluminescent immunoassay
Колич.характеристики :5 с
Место публикации : Russ. J. Bioorg. Chem.: MAIK NAUKA/INTERPERIODICA, 2004. - Vol. 30, Is. 4. - P327-331. - ISSN 1068-1620, DOI 10.1023/B:RUBI.0000037257.80835.7a
Примечания : Cited References: 16
Предметные рубрики: ESCHERICHIA-COLI
PURIFICATION
AEQUORIN
PROTEIN
CDNA
Ключевые слова (''Своб.индексиров.''): bioluminescent immunoassay--obelin--thyroid stimulating hormone
Аннотация: An efficient procedure for obelin conjugation with immunoglobulins was developed. The possibility was shown of using the resulting conjugates instead of a radioisotope label for the immunoassay of thyroid stimulating hormone in sera; the conjugates provide a sensitivity of 0.01 muIU/ml. The results of bioluminescent immunoassay (sera of 34 patients) satisfactorily correlate with the results of radioisotope assay (R 0.99).
WOS
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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) : 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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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKII Y.S., BONDAR V.S., TROFIMOV K.P., GITELZON I.I.
Заглавие : LUMINESCENCE OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN UNDER THE ACTION OF ACTIVE FORMS OF OXYGEN
Колич.характеристики :5 с
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1991. - Vol. 321, Is. 4. - С. 850-854. - ISSN 0002-3264
Примечания : Cited References: 8
Предметные рубрики: AEQUORIN
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondar V.S., Purtov K.V., Malikova N.P., Frank L.A., Illarionov B.A.
Заглавие : Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: MAIK NAUKA/INTERPERIODICA, 2001. - Vol. 66, Is. 9. - С. 1014-1018. - ISSN 0006-2979, DOI 10.1023/A:1012377827626
Примечания : Cited References: 21
Предметные рубрики: CDNA
EXPRESSION
AEQUORIN
SEQUENCE
CLONING
Ключевые слова (''Своб.индексиров.''): photoproteins--obelin--apoobelin mutants--bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein S-mutant A-mutant. This is consistent with rank of nucleophilicity SH OH CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.
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12.

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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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKII Y.S., BONDAR V.S., GITELZON I.I.
Заглавие : ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN
Колич.характеристики :4 с
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1991. - Vol. 321, Is. 1. - С. 214-217. - ISSN 0002-3264
Примечания : Cited References: 14
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
PROTEIN
PURIFICATION
EXTRACTION
PHIALIDIN
SEQUENCE
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., SERGEEV A.G., ILLARIONOV B.A., VERVOORT J..., HAGEN W.R.
Заглавие : CADMIUM-INDUCED LUMINESCENCE OF RECOMBINANT PHOTOPROTEIN OBELIN
Колич.характеристики :4 с
Место публикации : Biochim. Biophys. Acta-Bioenerg.: ELSEVIER SCIENCE BV, 1995. - Vol. 1231, Is. 1. - С. 29-32. - ISSN 0005-2728, DOI 10.1016/0005-2728(95)00059-R
Примечания : Cited References: 21
Предметные рубрики: AEQUORIN
Ключевые слова (''Своб.индексиров.''): photoprotein--obelin--cadmium--bioluminescence
Аннотация: It has been shown for the first time that Cd2+ ions induce substantial bioluminescence of a Ca2+-binding photoprotein: recombinant obelin. The optimum pH for the bioluminescent rr:action in the presence of Cd2+ ions is pH 6. The intensity, L, of the light emission for the Cd2+ ions is 75% of the intensity of the signal in the presence of Ca2+. The quantum yields of the reactions in the presence of Cd2+ and Ca2+ are 0.18 and 0.24 respectively. The slope of the straight line (between 5 and 90% of L,,) in the coordinates of log(L/(L(max) - L)) vs. log([Cd2+]) is 1.75 +/- 0.06, which indicates positive cooperative character of this reaction. At a concentration exceeding 1 . 10(-3) M, Cd2+ inhibits the bioluminescent reaction.
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L.A.
Заглавие : Ca2+-Regulated Photoproteins: Effective Immunoassay Reporters
Колич.характеристики :14 с
Коллективы :
Место публикации : Sensors: MDPI AG, 2010. - Vol. 10, Is. 12. - С. 11287-11300. - ISSN 1424-8220, DOI 10.3390/s101211287
Примечания : Cited References: 70. - This work was supported by the grant No. 76 of the Russian Academy of Sciences, Siberian Branch.
Предметные рубрики: POLYMERASE-CHAIN-REACTION
CYTOKINE MESSENGER-RNA
BIOLUMINESCENT IMMUNOASSAY
MYCOBACTERIUM-TUBERCULOSIS
BIOTINYLATED AEQUORIN
RECOMBINANT AEQUORIN
ANGSTROM RESOLUTION
FUSION PROTEIN
PCR ASSAY
OBELIN
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-regulated photoprotein--immunoassay--pcr-elisa--multiplex assay--re-engineered photoproteins
Аннотация: Ca2+-regulated photoproteins of luminous marine coelenterates are of interest and a challenge for researchers as a unique bioluminescent system and as a promising analytical instrument for both in vivo and in vitro applications. The proteins are comprehensively studied as to biochemical properties, tertiary structures, bioluminescence mechanism, etc. This knowledge, along with available recombinant proteins serves the basis for development of unique bioluminescent detection systems that are "self-contained", triggerable, fast, highly sensitive, and non-hazardous. In the paper, we focus on the use of photoproteins as reporters in binding assays based on immunological recognition element-bioluminescent immunoassay and hybridization immunoassay, their advantages and prospects.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Stepanyuk G.A., Golz S..., Markova S.V., Frank L.A., Lee J..., Vysotski E.S.
Заглавие : Interchange of aequorin and obelin bioluminescence color is determined by substitution of one active site residue of each photoprotein
Колич.характеристики :7 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2005. - Vol. 579, Is. 5. - С. 1008-1014. - ISSN 0014-5793, DOI 10.1016/j.febslet.2005.01.004
Примечания : Cited References: 49
Предметные рубрики: FIREFLY LUCIFERASE
SEQUENCE-ANALYSIS
CA2+-REGULATED PHOTOPROTEINS
CA2+-DISCHARGED PHOTOPROTEIN
VIOLET BIOLUMINESCENCE
INTRACELLULAR CALCIUM
ENDOPLASMIC-RETICULUM
ANGSTROM RESOLUTION
CRYSTAL-STRUCTURE
APOAEQUORIN CDNA
Ключевые слова (''Своб.индексиров.''): coelenterazine--calcium--reporter protein--mammalian expression--fluorescence spectrum
Аннотация: The bioluminescence spectra from the Ca2+-regulated photoproteins aequorin (lambda(max) = 469 nm) and obelin (lambda(max) = 482 nm) differ because aequorin has an H-bond from its Tyr82 to the bound coelenteramide, not present in obelin at the corresponding Phe88. Substitutions of this Phe88 by Tyr, Trp, or His shifted the obelin bioluminescence to shorter wavelength with F88Y having lambda(max) = 453 nm. Removal of the H-bond by the substitution of Y82F in aequorin shifted its bioluminescence to lambda(max) = 501 nm. All mutants were stable with good activity and were expressible in mammalian cells, thereby demonstrating potential for monitoring multiple events in cells using multi-color detection. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., MARKOVA S.V., BONDAR V.S., VYSOTSKY E.S., GITELSON J.I.
Заглавие : ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA
Колич.характеристики :3 с
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1992. - Vol. 326, Is. 5. - С. 911-913. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: AEQUORIN
PROTEIN
PHIALIDIN
CLONING
CA-2+
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Frank L..., Markova S..., Remmel N..., Vysotski E..., Gitelson I...
Заглавие : Bioluminescent signal system: bioluminescence immunoassay of pathogenic organisms
Колич.характеристики :6 с
Место публикации : Luminescence: JOHN WILEY & SONS LTD, 2007. - Vol. 22, Is. 3. - С. 215-220. - ISSN 1522-7235, DOI 10.1002/bio.952
Примечания : Cited References: 14
Предметные рубрики: AEQUORIN
AGENTS
OBELIN
ASSAYS
LABEL
Ключевые слова (''Своб.индексиров.''): obelin--bioluminescence immunoassay--infective agents
Аннотация: The Ca2+-regulated photoprotein obelin has been examined as a label for bioluminescence immunoassay of infective agents. The hepatitis B virus (HbsAg) and the bacteria Escherichia coli and Shigella sonnei lipopolysaccharide (LPS) were chosen as model antigens. Chemically synthesized obelin-corresponding antibody conjugates were used in a solid-phase microplate immunoassay. The sensitivities achieved by the assay were 0.25 ng/mL for S. sonnei LPS and 0.375 ng/mL for HbsAg. A novel, filter-based immunoassay to determine bacterial admixtures in the environment was proposed. The NanoCeram filters were effectively applied to 'trap' and pre-concentrate pathogens from samples under study for the purposes of further detection and measurement of the absorbed material by bioluminescence immunoassay. Copyright (C) 2007 John Wiley & Sons, Ltd.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ding, Bo-Wen, Eremeeva, Elena V., Vysotski, Eugene S., Liu, Ya-Jun
Заглавие : Luminescence Activity Decreases Whenv-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein-A Theoretical and Experimental Study
Колич.характеристики :14 с
Коллективы : National Natural Science Foundation of ChinaNational Natural Science Foundation of China [21911530094, 21673020, 21973005]; RFBRRussian Foundation for Basic Research (RFBR) [19-54-53004, 20-54-53011]; China Postdoctoral Science FoundationChina Postdoctoral Science Foundation [2018M630100]
Место публикации : Photochem. Photobiol.: WILEY, 2020. - Article in press. - ISSN 0031-8655, DOI 10.1111/php.13280. - ISSN 1751-1097(eISSN)
Примечания : Cited References:68. - This study was sponsored by the National Natural Science Foundation of China (Grant No. 21911530094, 21673020 and 21973005) and RFBR (Grant No. 19-54-53004 and 20-54-53011). Ding also thank the support from the China Postdoctoral Science Foundation (Grant No. 2018M630100).
Предметные рубрики: RECOMBINANT SEMISYNTHETIC AEQUORINS
OBELIN BIOLUMINESCENCE
MECHANISTIC
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analogv-CTZ. The latter is formed by adding a phenyl ring to the pi-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the pi-pi stacking interactions between the conjugated moiety ofv-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced byv-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments.
WOS
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ding B. -W., Eremeeva E. V., Vysotski E. S., Liu Y. -J.
Заглавие : Luminescence Activity Decreases When v-coelenterazine Replaces Coelenterazine in Calcium-Regulated Photoprotein—A Theoretical and Experimental Study
Место публикации : Photochem. Photobiol.: Blackwell Publishing Inc., 2020. - Article in press. - ISSN 00318655 (ISSN), DOI 10.1111/php.13280
Аннотация: Calcium-regulated photoproteins are found in at least five phyla of organisms. The light emitted by those photoproteins can be tuned by mutating the photoprotein and/or by modifying the substrate coelenterazine (CTZ). Thirty years ago, Shimomura observed that the luminescence activity of aequorin was dramatically reduced when the substrate CTZ was replaced by its analog v-CTZ. The latter is formed by adding a phenyl ring to the ?-conjugated moiety of CTZ. The decrease in luminescence activity has not been understood until now. In this paper, through combined quantum mechanics and molecular mechanics calculations as well as molecular dynamics simulations, we discovered the reason for this observation. Modification of the substrate changes the conformation of nearby aromatic residues and enhances the ?-? stacking interactions between the conjugated moiety of v-CTZ and the residues, which weakens the charge transfer to form light emitter and leads to a lower luminescence activity. The microenvironments of CTZ in obelin and in aequorin are very similar, so we predicted that the luminescence activity of obelin will also dramatically decrease when CTZ is replaced by v-CTZ. This prediction has received strong evidence from currently theoretical calculations and has been verified by experiments. © 2020 American Society for Photobiology
Scopus
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