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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gorokhovatsky A.Y., Shaloiko L.A., Bondar V.S., Vysotski E.S., Maximov E.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cell-free bioluminescent screening of translation inhibitors
Колич.характеристики :5 с
Место публикации : Biotechnol. Appl. Biochem.: PORTLAND PRESS, 1998. - Vol. 27. - С. 259-263. - ISSN 0885-4513
Примечания : Cited References: 21
Предметные рубрики: DIPHTHERIA-TOXIN
MESSENGER-RNA
SYSTEM
PROTEINS
Аннотация: The possibility of creating new screening methods with a cell-free translation system has been demonstrated with a quantitative determination of diphtheria toxin and some antibiotics (puromycin, kanamycin and tetracycline) as examples. The approach proposed follows from the ability of various substances to inhibit protein synthesis. We used a wheat-germ cell-free translation system stabilized by freeze-drying in the presence of trehalose with the mRNA of the Ca2+-activated photoprotein obelin as a reporter template. This freeze-dried cell-free translation system allows prolonged storage of the detecting system before it is required, increases the reproducibility of the results and simplifies the application procedure. The obelin mRNA extends the sensitivity of the method owing to the high sensitivity of detection of the synthesized protein.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : MATVEEV S.V., ILLARIONOV B.A., VYSOTSKI E.S., BONDAR V.S., MARKOVA S.V., ALAKHOV Y.B.
Заглавие : OBELIN MESSENGER-RNA - A NEW TOOL FOR STUDIES OF TRANSLATION IN CELL-FREE SYSTEMS
Колич.характеристики :6 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 231, Is. 1. - С. 34-39. - ISSN 0003-2697, DOI 10.1006/abio.1995.1499
Примечания : Cited References: 17
Предметные рубрики: MESSENGER-RNA
AEQUORIN
PROTEIN
CLONING
CDNA
Аннотация: Obelin mRNA obtained in vitro with the aid of SP6 RNA polymerase was translated in a wheat germ cell-free system, Only the polypeptide with a molecular mass of about 20 kDa was synthesized. The activation of apoobelin with a synthetic coelenterazine revealed a luminescence activity initiated by calcium. The specific activity was 3.6 +/- 0.4 x 10(15) photons per mg of the in vitro synthesized obelin (k = 6.9 s(-1)). The luminescence of the obelin was in a good correlation with the protein concentration calculated by the incorporation of [C-14]Leu. The determination of the amount of de novo synthesized obelin based on measurement of its luminescence is one-thousand times more sensitive than the approach based on the incorporation of labeled amino acid. Thus, obelin mRNA has some advantages for evaluating the efficiency of cell-free translation when compared with standard methods. (C) 1995 Academic Press, Inc.
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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) : 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) : 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) : 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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