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All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin [Text] / L. . Deng [et al.] // Protein Sci. - 2005. - Vol. 14, Is. 3. - P663-675, DOI 10.1110/ps.041142905. - Cited References: 46 . - ISSN 0961-8368

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   ANGSTROM RESOLUTION
   SEQUENCE-ANALYSIS
   CA2+-REGULATED PHOTOPROTEINS
   CA2+-DISCHARGED PHOTOPROTEIN
   LUMINESCENT PROTEIN
   MODULATED PROTEINS
   ELECTRON-DENSITY
   CLONING
   CDNA
Кл.слова (ненормированные):
bioluminescence -- EF-hand -- fluorescent protein -- proton relay -- calcium-binding loops -- aequorin -- obelin -- diffraction
Аннотация: The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7 Angstrom and 2.2 Angstrom. respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-proteins retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hydroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deng, L...; Vysotski, E.S.; Markova, S.V.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2013. - Vol. 12, Is. 6. - P1016-1024, DOI 10.1039/c3pp00002h. - 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. . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
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.

Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Visser, Antonie J. W. G.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Markova, Svetlana V.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Frank, L.A.; Visser, AJWG; van Berkel, WJH; Vysotski, E.S.

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Bioluminescent reporters for identification of gene allelic variants / V. V. Krasitskaya [et al.] // Russ. J. Bioorg. Chem. - 2012. - Vol. 38, Is. 3. - P298-305, DOI 10.1134/S1068162012030090. - Cited References: 13. - The authors thank the staff of Hematology Research Center (Krasnoyarsk Branch of Russian Academy of Medical Sciences) for providing DNA samples. The work was supported by the Integration Interdisciplinary Project of Siberian Branch of the Russian Academy of Sciences No. 76 and the Krasno yarsk Regional Fund for the support of scientific and technological activities. . - ISSN 1068-1620

РУБ Biochemistry & Molecular Biology + Chemistry, Organic
Рубрики:
COELENTERAZINE-BINDING PROTEIN
   RENILLA-MUELLERI
   LUCIFERASE
   PURIFICATION
   SUBSTRATE
   CLONING
   CDNA
Кл.слова (ненормированные):
SNP -- PEXT reaction -- obelin -- luciferase -- bioluminescent microassay
Аннотация: A method for single nucleotide polymorphism identification was developed, which was based on the primer extension reaction (PEXT) followed by bioluminescent solid-phase microassay. Recombinant Ca2+-regulated photoprotein obelin and coelenterazine-dependent Renilla muelleri luciferase were used as reporters. The study was performed as an example of SNP genotyping of the human F5 gene encoding human Factor V Leiden polymorphism 1691 G -> A (R506Q). Genomic DNA was amplified by PCR using primers flanking polymorphic site of 140 base pairs. PCR products were used as templates for two PEXT reactions using two primers containing 3'-terminal nucleotides, which were complementary to either normal or mutant alleles. If the template and allele-specific primer were completely complementary, the latter was elongated with DNA polymerase. The resulting extension product contained biotin residue due to the presence of biotinylated deoxyuridine triphosphate (B-dUTP) in the reaction mixture. The products were analyzed using obelin-streptavidin conjugates. The optimal PEXT-reaction conditions were found, which ensured a high reliability of SNP genotyping. A new approach to simultaneously revealing both alleles in one well was developed using two bioluminescent reporters. The efficiency of the proposed approach was shown in the study of clinical DNA samples.

Держатели документа:
[Krasitskaya, V. V.
Burakova, L. P.
Frank, L. A.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Akademgorodok, Russia
[Pyshnaya, I. A.] Russian Acad Sci, Siberian Branch, Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Krasitskaya, V.V.; Burakova, L.P.; Pyshnaya, I.A.; Frank, L.A.

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Ca2+-triggered coelenterazine-binding protein from Renilla as an enzyme-dependent label for binding assay [Text] / V. V. Krasitskaya [et al.] // Anal. Bioanal. Chem. - 2011. - Vol. 401, Is. 8. - P2573-2579, DOI 10.1007/s00216-011-5343-2. - Cited References: 17. - The work was supported by a "Leading Scientific School" (N 64987.2010.4) grant from the President of the Russian Federation and the "Molecular and Cell Biology" Program from the RAS. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
BIOLUMINESCENT IMMUNOASSAY
   LUCIFERASE
   PURIFICATION
   RENIFORMIS
   MUELLERI
   OBELIN
   PHOTOPROTEIN
   EXPRESSION
   SUBSTRATE
   CLONING
Кл.слова (ненормированные):
Ca2+-triggered coelenterazine-binding protein (CBP) -- Renilla muelleri luciferase -- Bioluminescent solid-phase microassay
Аннотация: The recombinant Ca2+-triggered coelenterazine-binding protein (CBP) from Renilla muelleri was investigated as a biospecifically labeled molecule for in vitro assay applications. The protein was shown to be stable in solutions in the frozen state, as well as stable under heating and to chemical modifications. Conjugates with biotin, oligonucleotide, and proteins were obtained and applied as biospecific molecules in a solid-phase microassay. CBP detection was performed with intact (no modifications were made) Renilla luciferase in the presence of calcium, and the detection limit was found to be 75 amol. Model experiments indicate that this approach shows much promise, especially with regard to the development of multianalytical systems.

Держатели документа:
[Korneeva, S. I.
Kudryavtsev, A. N.
Frank, L. A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Krasitskaya, V. V.
Markova, S. V.
Stepanyuk, G. A.
Frank, L. A.] Russian Acad Sci SB, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Krasitskaya, V.V.; Korneeva, S.I.; Kudryavtsev, A.N.; Markova, S.V.; Stepanyuk, G.A.; Frank, L.A.

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Cloning and expression of cDNA for a luciferase from the marine copepod Metridia longa - A novel secreted bioluminescent reporter enzyme [Text] / S. V. Markova [et al.] // J. Biol. Chem. - 2004. - Vol. 279, Is. 5. - P3212-3217, DOI 10.1074/jbc.M309639200. - Cited References: 37 . - ISSN 0021-9258

РУБ Biochemistry & Molecular Biology
Рубрики:
VARGULA-HILGENDORFII LUCIFERASE
   GREEN FLUORESCENT PROTEIN
   GENE-EXPRESSION
   FIREFLY LUCIFERASE
   PROMOTER ACTIVITY
   MAMMALIAN-CELLS
   RECEPTOR
   CANCER
   PHOTOPROTEINS
   LUMINESCENCE
Аннотация: Metridia longa is a marine copepod from which a blue bioluminescence originates as a secretion from epidermal glands in response to various stimuli. We demonstrate that Metridia luciferase is specific for coelenterazine to produce blue light (lambda(max)=480 nm). Using an expression cDNA library and functional screening, we cloned and sequenced the cDNA encoding the Metridia luciferase. The cDNA is an 897-bp fragment with a 656-bp open reading frame, which encodes a 219-amino acid polypeptide with a molecular weight of 23,885. The polypeptide contains an N-terminal signal peptide of 17 amino acid residues for secretion. On expression of the Metridia luciferase gene in mammalian Chinese hamster ovary cells the luciferase is detected in the culture medium confirming the existence of a naturally occurring signal peptide for secretion in the cloned luciferase. The novel secreted luciferase was tested in a practical assay application in which the activity of A2a and NPY2 G-protein-coupled receptors was detected. These results clearly suggest that the secreted Metridia luciferase is well suited as a reporter for monitoring gene expression and, in particular, for the development of novel ultra-high throughput screening technologies.

Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
Bayer AG, Pharma Res Mol Screening Technol, D-42096 Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Golz, S...; Frank, L.A.; Kalthof, B...; Vysotski, E.S.

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Cloning and molecular organization of the polyhydroxyalkanoic acid synthase gene (phaC) of Ralstonia eutropha strain B5786 / I. V. Kozhevnikov [et al.] // Applied Biochemistry and Microbiology. - 2010. - Vol. 46, Is. 2. - P140-147, DOI 10.1134/S0003683810020031 . - ISSN 0003-6838
Кл.слова (ненормированные):
Aeromonas punctata -- Cupriavidus necator -- Ectothiorhodospira shaposhnikovii -- Pseudomonas -- Pseudomonas sp. 61-3 -- Rhodococcus -- Rhodococcus ruber -- Rhodospirillum rubrum -- Thiococcus pfennigii
Аннотация: Class I polyhydroxyalkanoic acid (PHA) synthase gene (phaC) of Ralstonia eutropha strain B5786 was cloned and characterized. R. eutropha B5786 features the ability to synthesize multicomponent PHAs with short- and medium-chain-length monomers from simple carbohydrate substrate. A correlation was made between the molecular structure of PHA synthase and substrate specificity and the ability of strain-producers to accumulate PHAs of this or that structure. A strong similarity of PHA synthase of R. eutropha strain B5786 with PHA synthase of R. eutropha strain H16, which, as opposed to strain B5786, enables to incorporate medium chain length PHAs if hexanoate is used as carbon source, exhibited 99%. A correlation between the structure of PHA synthase of B5786 strain with synthases of microorganisms which synthesize short and medium chain length PHAs similarly to B5786 strain, showed an identity level from 26 to 41% (homology with synthase of Rhodospirillum rubrum makes 41%, Ectothiorhodospira shaposhnikovii makes 26%, Aeromonas punctata makes 40%, Thiococcus pfennigii makes 28%, Rhodococcus ruber makes 38%, and with PhaCl and PhaC2 synthases of Pseudomonas sp. 61-3 makes 34 and 37%, respectively). This allows for speaking about the absence of a direct connection between the molecular organization of PHA synthases and their functional abilities, namely, the ability to synthesize PHAs of a particular composition. В© 2010 Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Siberian Federal University, Krasnoyarsk 660041, Russian Federation
Institute of Biophysics of Siberian Branch, Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Molecular Microbiology and Biotechnology, B-48149 Munster, Germany : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kozhevnikov, I.V.; Volova, T.G.; Hai, T.; Steinbuchel, A.

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Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase [Text] / M. S. Titushin [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 2. - P189-196, DOI 10.1039/b713109g. - Cited References: 41 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
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.

Держатели документа:
[Titushin, Maxim S.
Markova, Svetlana V.
Frank, Ludmila A.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Lee, John
Vysotski, Eugene S.] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Markova, S.V.; Frank, L.A.; Malikova, N.P.; Stepanyuk, G.A.; Lee, J...; Vysotski, E.S.

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Coelenterazine-binding protein of Renilla muelleri: Cloning and determination of three-dimensional structure [Text] / G. A. Stepanyuk [et al.] // Luminescence. - 2006. - Vol. 21, Is. 5. - P292-292. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
RAS, SB, Inst Biophys, Pathobiol Lab, Krasnoyarsk 660036, Russia
Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Stepanyuk, G.A.; Markova, S.V.; Liu, Z.J.; Frank, L.A.; Lee, J...; Vysotski, E.S.; Wang, C...

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Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase [Text] / G. A. Stepanyuk [et al.] // Anal. Bioanal. Chem. - 2010. - Vol. 398, Is. 4. - P1809-1817, DOI 10.1007/s00216-010-4106-9. - Cited References: 39. - This work was supported by grant 09-04-12022 of the Russian Foundation for Basic Research, "Molecular and Cell Biology" program of Russian Academy of Sciences, by the SB RAS grant No. 2, and by the SB RAS Lavrentiev grant for Young Scientists. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
GREEN-FLUORESCENT PROTEIN
   BIOLUMINESCENT REPORTER
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   RECOMBINANT OBELIN
   GENE-EXPRESSION
   IN-VIVO
   CDNA
   CLONING
   PURIFICATION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Calcium -- Imaging
Аннотация: It has been shown that the coelenterazine analog, coelenterazine-v, is an efficient substrate for a reaction catalyzed by Renilla luciferase. The resulting bioluminescence emission maximum is shifted to a longer wavelength up to 40 nm, which allows the use of some "yellow" Renilla luciferase mutants for in vivo imaging. However, the utility of coelenterazine-v in small-animal imaging has been hampered by its instability in solution and in biological tissues. To overcome this drawback, we ligated coelenterazine-v to Ca2+-triggered coelenterazine-binding protein from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The coelenterazine-v bound within coelenterazine-binding protein has revealed a greater long-term stability at both 4 and 37 degrees C. In addition, the coelenterazine-binding protein ligated by coelenterazine-v yields twice the total light over free coelenterazine-v as a substrate for the red-shifted R. muelleri luciferase. These findings suggest the possibility for effective application of coelenterazine-v in various in vitro assays.

Держатели документа:
[Stepanyuk, Galina A.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Unch, James] Promega Biosci LLC, San Luis Obispo, CA 93401 USA
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Unch, J...; Malikova, N.P.; Markova, S.V.; Lee, J...; Vysotski, E.S.

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10.

Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course [Text] / N. G. Berestovskaya [et al.] // Anal. Biochem. - 1999. - Vol. 268, Is. 1. - P72-78, DOI 10.1006/abio.1998.3051. - Cited References: 22 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
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.

Держатели документа:
Russian Acad Sci, Branch Inst Bioorgan Chem, Pushchino 142292, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Tech Univ Berlin, Inst Biochem & Mol Biol, D-10587 Berlin, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Berestovskaya, N.G.; Shaloiko, L.A.; Gorokhovatsky, A.Y.; Bondar, V.S.; Vysotski, E.S.; Maximov, J.E.; von Doehren, H...; Alakhov, Y.B.

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11.

Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course [Text] / N. G. Berestovskaya [et al.] // Anal. Biochem. - 1999. - Vol. 268, Is. 1. - P. 72-78, DOI 10.1006/abio.1998.3051. - Cited References: 22 . - ISSN 0003-2697

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Analytical
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
Держатели документа:
Russian Acad Sci, Branch Inst Bioorgan Chem, Pushchino 142292, Russia
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Tech Univ Berlin, Inst Biochem & Mol Biol, D-10587 Berlin, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Berestovskaya, N.G.; Shaloiko, L.A.; Gorokhovatsky, A.Y.; Bondar, V.S.; Vysotski, E.S.; Maximov, J.E.; von Doehren, H...; Alakhov, Y.B.

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12.

Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 angstrom: Why it is not a calcium-regulated photoprotein [Text] / G. A. Stepanyuk [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 4. - P442-447, DOI 10.1039/b716535h. - Cited References: 49 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
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.

Держатели документа:
[Liu, Zhi-Jie] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[Stepanyuk, Galina A.
Lee, John
Vysotski, Eugene S.
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Markova, Svetlana S.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Markova, S.S.; Frank, L.A.; Lee, J...; Vysotski, E.S.; Wang, B.C.

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13.

Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha B5786 [Text] / T. G. Volova [et al.] // Appl. Biochem. Microbiol. - 2004. - Vol. 40, Is. 2. - P. 170-177, DOI 10.1023/B:ABIM.0000018921.04863.d5. - Cited References: 27 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
POLY-BETA-HYDROXYBUTYRATE
   ORGANISM ALCALIGENES-EUTROPHUS
   ESCHERICHIA-COLI
   PHB
   POLY(3-HYDROXYBUTYRATE)
   BIOSYNTHESIS
   CLONING
   GENES
   CHAIN
   H16
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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14.

Effect of environmental factors on the expression of the catabolite-dependent lux-operon borne by a recombinant plasmid / E. E. Maksimova [и др.] // Mikrobiologiya. - 1998. - Vol. 67, Is. 2. - С. 170-175 . - ISSN 0026-3656
Кл.слова (ненормированные):
Catabolite repression -- Environmental factors -- Escherichia coli -- Introduction into model ecosystems -- Lux-operon -- Recombinant plasmid -- Regulation of expression -- recombinant DNA -- article -- bacterial gene -- chemoluminescence -- culture medium -- Escherichia coli -- gene expression regulation -- genetics -- microbiology -- molecular cloning -- operon -- plasmid -- Chemiluminescent Measurements -- Cloning, Molecular -- Culture Media -- DNA, Recombinant -- Escherichia coli -- Gene Expression Regulation, Bacterial -- Genes, Bacterial -- Operon -- Plasmids -- Water Microbiology
Аннотация: Expression of the lux-genes cloned on the recombinant plasmid pPHL7 (Ap rLux +) in Escherichia coli Z905 cells was studied in various environments, including model aquatic ecosystems. Expression of the lux-genes strongly depended on the nutritional status of the medium. In particular, the cultivation of cells in nutrient-rich medium favored the maintenance of the initial level of expression of the lux-operon, whereas nutrient limitation induced recombinant cell variants with an impaired control of the catabolite-dependent luxoperon. On the other hand, long-term laboratory cultivation of the recombinant strain in nutrient-deficient media or its long-term life in model aquatic ecosystems led to the accumulation of cells with a stringent control on the cloned lux-genes in the bacterial population. The presence of the selective factor (ampicillin) in the medium had no significant effect on the expression of the lux-operon.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Maksimova, E.E.; Popova, L.Yu.; Shpagina, V.V.; Belyavskaya, V.A.; Pechurkin, N.S.

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15.

Expression of lux-genes as an indicator of metabolic activity of cells in model ecosystem studies [Text] / A. N. Boyandin, L. Y. Popova ; ed. M Nelson [et al.] // SPACE LIFE SCIENCES: CLOSED ARTIFICIAL ECOSYSTEMS AND LIFE SUPPORT SYSTEMS. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON-ELSEVIER SCIENCE LTD, 2003. - Vol. 31: Meeting of F4 1 Session of the 34th Scientific Assembly of COSPAR (OCT, 2002, HOUSTON, TEXAS), Is. 7. - P. 1839-1845, DOI 10.1016/S0273-1177(03)00014-0. - Cited References: 8 . - ISBN 0273-1177

РУБ Engineering, Aerospace + Astronomy & Astrophysics + Ecology + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

Аннотация: Quick response to different impacts and easy measurement make the luminescent systems of luminous bacteria an object convenient for application in various fields. Cloning of gene luminescence in different organisms is currently used to study both the survival of microbial cells and the effect of different factors on their metabolic activity, including the environment. A primary test-object in estimating bacteriological contamination of water bodies, Escherichia coli, can be conveniently used as an indicator of bactericidal properties of aquatic ecosystems. The application of Escherichia coli Z905/pPHL7 (lux(+)) as a marker microorganism can facilitate monitoring the microbiological status of closed biocenoses, including systems with higher organisms. The investigation of various parameters of microecosystems (carbon nutrition type, concentrations of inorganic ions and toxic compounds) shows that the recombinant strain E. coli Z905/pPHL7 can be effectively used as a marker. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Boyandin, A.N.; Popova, L.Y.; Nelson, M \ed.\; Pechurkin, NS \ed.\; Dempster, WF \ed.\; Somova, LA \ed.\; Somo, , LA \ed.\

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16.

Green-fluorescent protein from the bioluminescent jellyfish Clytia gregaria: cDNA cloning, expression, and characterization of novel recombinant protein [Text] / S. V. Markova [et al.] // Photochem. Photobiol. Sci. - 2010. - Vol. 9, Is. 6. - P757-765, DOI 10.1039/c0pp00023j. - 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). . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
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.

Держатели документа:
[Markova, Svetlana V.
Burakova, Ludmila P.
Frank, Ludmila A.
Korostileva, Kseniya A.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Frank, Ludmila A.
Korostileva, Kseniya A.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Golz, Stefan] Bayer Schering Pharma AG, BSP GDD GTR TD GT, D-42096 Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Frank, L.A.; Golz, S...; Korostileva, K.A.; Vysotski, E.S.

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17.

Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase / E. V. Eremeeva, S. V. Markova, E. S. Vysotski // Dokl. Biochem. Biophys. - 2013. - Vol. 450, Is. 1. - P147-150, DOI 10.1134/S1607672913030095. - Cited References: 14. - This work was supported by the Ministry of Education and Science of the Russian Federation (Government Contract no. 16.512.11.2141) and Council of the President of the Russian Federation on Grants and State Support of Leading Scientific Schools (project no. NSh-64987.2010.4). . - ISSN 1607-6729

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
   GENE-EXPRESSION
   CDNA
   CLONING
   BIOLUMINESCENCE
   RENIFORMIS

Scopus
Держатели документа:
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
[Eremeeva, E. V.
Markova, S. V.
Vysotski, E. S.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Svobodnyi pr. 79, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; Vysotski, E.S.

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18.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- anisotropy -- antenna -- article -- bioluminescence -- complex formation -- energy transfer -- enzyme active site -- enzyme kinetics -- nonhuman -- priority journal -- protein protein interaction -- spectroscopy -- vibrionaceae -- Bacterial Proteins -- Carrier Proteins -- Cloning, Molecular -- Dithionite -- Flavin Mononucleotide -- Kinetics -- Luciferases -- Luminescent Measurements -- Luminescent Proteins -- Models, Structural -- Photobacterium -- Protein Binding -- Protein Conformation -- Recombinant Proteins -- Spectrophotometry -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Photobacterium leiognathi -- Vibrio fischeri -- Vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.

Scopus
Держатели документа:
Department of Biochemistry, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Acad. of Sci. of Russia, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M.; Gibson, B.G.; Lee, J.

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19.

ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA [Текст] / B. A. ILLARIONOV [и др.] // Dokl. Akad. Nauk. - 1992. - Vol. 326, Is. 5. - С. 911-913. - Cited References: 12 . - ISSN 0869-5652

РУБ Multidisciplinary Sciences
Рубрики:
AEQUORIN
   PROTEIN
   PHIALIDIN
   CLONING
   CA-2+
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
ILLARIONOV, B.A.; MARKOVA, S.V.; BONDAR, V.S.; VYSOTSKY, E.S.; GITELSON, J.I.

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20.