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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.
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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. - С. 72-78. - 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.
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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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKI E.S., TROFIMOV C.P., BONDAR V.S., FRANK L.A., MARKOVA S.V., ILLARIONOV B.A.
Заглавие : MN2+-ACTIVATED LUMINESCENCE OF THE PHOTOPROTEIN OBELIN
Место публикации : Arch. Biochem. Biophys.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 316, Is. 1. - С. 92-99. - 8. - ISSN 0003-9861, DOI 10.1006/abbi.1995.1014
Примечания : Cited References: 38
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
CA-2+-ACTIVATED PHOTOPROTEIN
MESSENGER-RNA
BEROE-OVATA
AEQUORIN
PURIFICATION
PROTEIN
CDNA
EXTRACTION
Аннотация: The light emission of obelin may be initiated by Mn2+ under alkaline conditions. The luminescence takes place in a pH range from 7 to 12 with a sharp optimum at 11.75. The first-order rate constant for Mn2+-activated luminescence decay is more than 9 s(-1), while that for Ca2+-activated luminescence decay is only 6.9 s(-1). The Mn2+ concentration-effect curve for obelin determined with simple dilutions of manganese salt is a sigmoid curve, The slope of the curve is moderately dependent on the pH and was not more than 1 within the pH range tested. The maximal light emission, which is initiated by 3.6 X 10(-5) M Mn2+ at pH 11.75 was about 10% of the maximal Ca2+-activated luminescence. Mg2+ ions inhibit the Mn2+-activated luminescence of obelin. The addition of OH. and O-2(-) scavengers did not influence the Mn2+-activated luminescence, but when singlet oxygen quenchers were added, the Mn2+-dependent light emission was inhibited. This suggests that the O-1(2) might be formed and itself be responsible for chromophore oxidation attended with light emission. NEM and Na2S2O4 inhibit the Mn2+-initiated light emission of obelin completely, showing that endogenous hydroperoxide and SH-group(s) of the photoprotein are essential for both Ca2+-activated and Mn2+-activated light emission of obelin. (C) 1995 Academic Press, Inc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Vysotski E.S., Blinks J.R., Burakova L.P., Wang B.C., Lee J...
Заглавие : Obelin from the bioluminescent marine hydroid Obelia geniculata: Cloning, expression, and comparison of some properties with those of other Ca2+-regulated photoproteins
Колич.характеристики :10 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2002. - Vol. 41, Is. 7. - С. 2227-2236. - ISSN 0006-2960, DOI 10.1021/bi0117910
Примечания : Cited References: 54
Предметные рубрики: AMINO-ACID-SEQUENCE
CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
CA-2+-ACTIVATED PHOTOPROTEIN
LUMINESCENT PROTEIN
BINDING-PROTEIN
BEROE-OVATA
AEQUORIN
CDNA
PURIFICATION
Аннотация: A cDNA encoding the Ca2+-regulated photoprotein of the bioluminescent marine hydroid Obelia geniculata was cloned and sequenced. The cDNA is a 774 bp fragment containing two overlapping open reading frames, one of which contained 585 bp encoding a 195 amino acid polypeptide which obviously has the primary structure of the apoprotein of a calcium-regulated photoprotein. Many of the residues are identical to those in other Ca2+-regulated photoproteins: 86% compared with that from Obelia longissima, 76% with that from Clytia (Phialidium), 64% with that from Aequorea, and 64% with that from Mitrocoma (Halistaura). The obelin from O. geniculata was overexpressed in Escherichia coli, refolded from inclusion bodies, and purified. The yield of highly purified recombinant protein was 55-80 mg/L of LB medium. O. geniculata obelin has absorption maxima at 280 and 460 nm and a shoulder at approximately 310 nm. The calcium-discharged protein loses visible absorption but exhibits a new absorption maximum at 343 nm. The bioluminescence of the obelin from O. geniculata is blue (lambda(max) = 495 nm). In contrast, the fluorescence of the calcium-discharged protein is yellow-green (lambda(max) = 520 nm; excitation at 340 nm). This is in sharp contrast to aequorin in which the bioluminescence and fluorescence emission spectra of the calcium-discharged protein are almost identical (lambda(max) = 465 nm). The Ca2+ concentration-effect curve for O. geniculata obelin is similar to those of many other photoproteins: at [Ca2+] below approximately 10(-8) M, calcium-independent luminescence is observed, and at [Ca2+] approximately 10(-3) M, the luminescence reaches a maximum. Between these extremes, the curve spans a vertical range of almost 8 log units with a maximum slope on a log-log plot of about 2.5. In the absence of Mg2+ the rate constant for the rise of bioluminescence determined by the stopped-flow technique is about 450 s(-1). The effects of Mg2+ on the kinetics of bioluminescence are complicated, but at all concentrations studied they are relatively small compared to the corresponding effects on aequorin luminescence. At least with respect to speed and sensitivity to Mg2+, the obelins from both O. longissima and O. geniculata would appear to be more suitable than aequorin for use as intracellular Ca2+ indicators.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarionov B.A., Frank L.A., Illarionova V.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator
Колич.характеристики :27 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - С. 223-249. - ISSN 0076-6879
Примечания : Cited References: 58
Предметные рубрики: PHOTOPROTEIN OBELIN
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
DIRECTED MUTAGENESIS
SEQUENCE-ANALYSIS
HYDROID OBELIA
AEQUORIN
PROTEIN
BIOLUMINESCENCE
LUMINESCENCE
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., BONDAR V.S., ILLARIONOVA V.A., VYSOTSKI E.S.
Заглавие : SEQUENCE OF THE CDNA-ENCODING THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Gene: ELSEVIER SCIENCE BV, 1995. - Vol. 153, Is. 2. - С. 273-274. - 2. - ISSN 0378-1119, DOI 10.1016/0378-1119(94)00797-V
Примечания : Cited References: 6
Предметные рубрики: CA-2+-ACTIVATED PHOTOPROTEIN
AEQUORIN
CLONING
Ключевые слова (''Своб.индексиров.''): bioluminescence--calcium--gene--plasmid--marine coelenterates
Аннотация: A cDNA clone encoding the Ca2+-activated photoprotein, obelin (Obl), from Obelia longissima was sequenced. The nucleotide (nt) sequence contained two long overlapping open reading frames (ORFs), one of which encoded apoobelin (apoObl). The deduced amino acid (aa) sequence of apoObl revealed that this 195-aa protein has three EF-hand structures that are characteristic for Ca2+-binding domains. Strong aa homology was shown among apoObl, apoaequorin and apoclytin. The second ORF present in the obl cDNA consists of 139 codons and encodes a very basic protein with a calculated pI of 10.56 and a molecular mass of 16153 Da.
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