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A conflict: Induction-inhibition of luminescence in the expression of lux-genes in transgenic bacteria [Текст] / D. V. Lesnyak, L. Y. Popova // Biofizika. - 2002. - Vol. 47, Is. 6. - P. 1059-1063. - Cited References: 12 . - ISSN 0006-3029

РУБ Biophysics

Кл.слова (ненормированные):
salicylate, naphtalene concentration -- bacterial bioluminescence, biodegradation
Аннотация: The relationship between the induction of the luminescent operon of lux-genes fused with the naphthalene and salicylate degradation genes and the inhibition of light emission caused by these compounds was studied. The quantitative correlations between these processes manifest themselves in the fact that light intensity linearly increased in a narrow concentration range of the inductor and then decreased due to the inhibition of the luminescence reaction itself, which is not related to the regulation of expression of lux-genes.

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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:
Lesnyak, D.V.; Popova, L.Y.

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A test system for tick-borne encephalitis virus detection based on bioluminescent immunoassay / A. N. Kudryavtsev, L. P. Burakova, K. A. Barinova, L. A. Frank // J. Sib. Fed. Univ. - Biol. - 2020. - Vol. 13, Is. 3. - С. 310-321, DOI 10.17516/1997-1389-0296 . - ISSN 1997-1389
Кл.слова (ненормированные):
Bioluminescent microassay -- Hybrid protein 14D5a-Rm7 -- Tick-borne encephalitis virus (TBEV)
Аннотация: The tick-borne encephalitis virus (TBEV) is the causative agent of one of the most severe human neuroinfections. The infection transmitted by ixodid ticks is spread throughout the forest and forest-steppe zones of the temperate climatic belt of the Eurasian continent, including the Siberian region of the Russian Federation. Despite the availability of commercial analytical systems for the detection of TBEV, the task of developing approaches to a quick and reliable analysis that can be performed routinely, particularly in environmental studies, remains topical. A solid-phase bioluminescent immunoassay for determining the tick-borne encephalitis virus (TBEV) in ticks was developed. The assay is based on the hybrid protein consisting of a modified thermostable version of Renilla muelleri luciferase and a single-chain mini-antibody to protein E. This unique protein had been obtained and investigated by the authors earlier. The current study describes the expression of the hybrid protein in two different strains of recombinant E. coli cells. The optimal conditions for obtaining a highly purified protein were found. The bioluminescent reaction of the luciferase domain was triggered with the help of the stable natural form of the substrate, a Ca-dependent coelenterazine-binding protein, the recombinant variant of which was obtained by the authors. The conditions for production and storage of the immunoassay components (the hybrid protein, the stable form of the luciferase substrate, and activated microplates) were determined. Using the developed test system, more than 900 tick samples were analyzed for TBEV. In terms of sensitivity (89.5%) and specificity (98.9%), the proposed method is not inferior to colorimetric detection and is much simpler and faster than the latter. © Siberian Federal University. All rights reserved.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, FRC Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kudryavtsev, A. N.; Burakova, L. P.; Barinova, K. A.; Frank, L. A.

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Analytical expression of the dependence of the productivity of micro-algae on temperature / L. I. Slobodskoi [et al.] // Biophysics. - 1969. - Vol. 14, Is. 1. - P210-214 . - ISSN 0006-3509

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

Доп.точки доступа:
Slobodskoi, L.I.; Sid'ko, F.Ya.; Belyanin, V.I.; Alypov, V.F.; Beresnev, G.F.

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Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine [Text] / Z. J. Liu [et al.] // Biochem. Biophys. Res. Commun. - 2003. - Vol. 311, Is. 2. - P433-439, DOI 10.1016/j.bbrc.2003.09.231. - Cited References: 29 . - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENT PROTEIN
   VIOLET BIOLUMINESCENCE
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   PURIFICATION
   REFINEMENT
   EXPRESSION
Кл.слова (ненормированные):
photoprotein -- bioluminescence -- atomic resolution -- EF-hand
Аннотация: The spatial structure of the Ca2+-regulated photoprotein obelin has been solved to resolution of 1.1 Angstrom. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73 Angstrom resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca2+, the electron densities of both oxygen atoms became equally intense. In addition, one Ca2+ was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms. (C) 2003 Elsevier Inc. All rights reserved.

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:
Liu, Z.J.; Vysotski, E.S.; Deng, L...; Lee, J...; Rose, J...; Wang, B.C.

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Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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Bioluminescent detection probe for tick-borne encephalitis virus immunoassay [Text] / L. P. Burakova [et al.] // Anal. Bioanal. Chem. - 2015. - Vol. 407, Is. 18. - P5417-5423, DOI 10.1007/s00216-015-8710-6. - Cited References:19. - The work was supported by the Russian Academy of Sciences, Siberian Branch, within the framework of the Interdisciplinary Integration Project No. 139 and the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1). . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
COELENTERAZINE-BINDING PROTEIN
ENZYME-IMMUNOASSAY
RENILLA-MUELLERI
Кл.слова (ненормированные):
Tick-borne encephalitis virus -- Single-chain antibody -- Luciferase -- Immunoassay
Аннотация: To facilitate the detection of the tick-borne encephalitis virus (TBEV), the causative agent of one of the most severe human neuroinfections, we have developed an immunoassay based on bioluminescent hybrid protein 14D5a-Rm7 as a detection probe. The protein containing Renilla luciferase as a reporter and a single-chain variable fragment (scFv) of murine immunoglobulin to TBEV as a recognition element was constructed, produced by bacterial expression, purified, and tested. Both domains were shown to reveal their specific biological properties-affinity to the target antigen and bioluminescent activity. Hybrid protein was applied as a label for solid-phase immunoassay of the antigens, associated with the tick-borne encephalitis virus (native glycoprotein E or extracts of the infected strain of lab ticks). The assay demonstrates high sensitivity (0.056 ng of glycoprotein E; 10(4)-10(5) virus particles or 0.1 pg virions) and simplicity and is competitive with conventional methods for detection of TBEV.

WOS,
Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Poliomyelitis & Viral Encephalitides, Moscow 142782, Russia.
Res Inst Nat Foci Infect, Omsk 644080, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Kudryavtsev, Alexander N.; Stepanyuk, Galina A.; Baykov, Ivan K.; Morozova, Vera V.; Tikunova, Nina V.; Dubova, Maria A.; Lyapustin, Victor N.; Yakimenko, Valeri V.; Frank, Ludmila A.; Russian Academy of Sciences, Siberian Branch [139]; Russian Academy of Sciences [VI 57.1.1]

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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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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.

Conflict: induction-inhibition of transgene bacteria luminescence in studying expression of lux-genes / D. V. Lesniak, L. I. Popova // Biofizika. - 2002. - Vol. 47, Is. 6. - P. 1059-1063 . - ISSN 0006-3029
Кл.слова (ненормированные):
naphthalene derivative -- salicylic acid derivative -- article -- bacterial gene -- chemistry -- chemoluminescence -- culture medium -- Escherichia coli -- gene expression regulation -- genetics -- metabolism -- Pseudomonas fluorescens -- transgene -- Chemiluminescent Measurements -- Culture Media -- Escherichia coli -- Gene Expression Regulation, Bacterial -- Genes, Bacterial -- Naphthalenes -- Pseudomonas fluorescens -- Salicylates -- Transgenes
Аннотация: The relationship between the induction of the luminescent operon of lux-genes fused with the naphthalene and salicylate degradation genes and the inhibition of light emission caused by these compounds was studied. The quantitative correlations between these processes manifest themselves in the fact that light intensity linearly increased in a narrow concentration range of the inductor and then decreased due to the inhibition of the luminescence reaction itself, which is not related to the regulation of expression of lux-genes.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk-36, Akademgorodok, 660036 Russia. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Lesniak, D.V.; Popova, L.I.

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11.

Controlled expression of bacterial luminescence genes cloned in a multicopy recombinant plasmid [Text] / E. E. Maksimova [et al.] // Microbiology. - 1997. - Vol. 66, Is. 2. - P. 184-187. - Cited References: 17 . - ISSN 0026-2617

РУБ Microbiology
Рубрики:
GENETICALLY-MODIFIED MICROORGANISMS
BIOLUMINESCENCE
ENVIRONMENT
Кл.слова (ненормированные):
recombinant plasmid -- Escherichia coli -- luminescence -- catabolite repression
Аннотация: Luminescence and growth responses of the recombinant strain Escherichia coil Z905 (Ap(r)Lux(+)) to different concentrations of ampicillin depended on the source of carbon and energy. When glycerol was used as the substrate, the intensity of luminescence rose with the ampicillin concentration in the medium. Glucose caused catabolite repression of cell luminescence up to the late stationary phase, and ampicillin enhanced this effect. The feasibility of controlling the expression of cloned lux genes was shown.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Maksimova, E.E.; Popova, L.Y.; Kargatova, T.V.; Shpagina, V.V.

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12.

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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13.

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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14.

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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15.

Dietary buckwheat enhances sirtuin1 without calorie restriction / S. Pande, R. Ranjan, A. N. Shuvaev [et al.] // J. Cereal Sci. - 2020. - Vol. 94. - Ст. 103004, DOI 10.1016/j.jcs.2020.103004. - Cited References:22. - This work was supported by the Russian Foundation for Basic Research (RFBR) [Grant No. 16-06-00-439] and by the Russian Ministry of Education, Post-Doctoral Program of Project "5-100" [Grant No. M 2.2.3]. . - ISSN 0733-5210. - ISSN 1095-9963

РУБ Food Science & Technology
Рубрики:
LIFE-SPAN
   STRESS
   FLOUR
   RATS
Кл.слова (ненормированные):
Dietary buckwheat -- SIRT1 expression -- Calorie restriction -- Male wistar -- rats
Аннотация: In the present investigation, the role of dietary intervention in male Wistar rats (n = 8, 3 groups) was studied to observe absolute sirtuin 1 (SIRT1) levels (expressed as ng mg(-1) total protein) in serum, stomach, liver, and kidney. Dietary buckwheat at 30% (w/w) level of incorporation in the standard diet (Buckwheat Enriched Diet, BED) improved SIRT1 with values 0.933 +/- 0.05, 210 +/- 7, 63.26 +/- 4, and 69.89 +/- 3 in serum, stomach, liver, and kidney respectively when compared to the respective control values of 0.536 +/- 0.03, 156 +/- 23.3, 31.07 +/- 2 and 47.11 +/- 4. Moreover, BED though isocaloric to CR diet, led to weight gain (g) by 63.11 +/- 3.8, ca. 10%, and 40% higher than control (56.27 +/- 5.6) and CR (45.05 +/- 4.1) diet groups. A marked rise in Feed Efficiency Ratio (FER) by ca. 37% while a 30% decrease in Feed Conversion Ratio (FCR) was observed for the BED group which supports unexpected weight gain in rats post-dietary intervention. The results justify the superior nutritional profile of buckwheat laden with essential nutrients, essential proteins, and bioactives. In contrast, Calorie Restriction (CR) resulted in a decline of the total protein content in circulation by 19%, while reduction of total protein in stomach, liver, and kidney was estimated to be 95%, 35.2%, and 27% respectively though SIRT1 values were comparatively the highest in all the samples studied. A 30-fold enhancement of SIRT1 in stomach post CR is presumed to counter enhanced stress in gastric tissues. Therefore, mild to moderate expression of SIRT1 may confer beneficial effects such as delayed aging and stress resistance but exceedingly high SIRT1 may evoke increased oxidative stress.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Dept Biophys, Lab Bioluminescent Biotechnol, Svobodny Prospect 79, Krasnoyarsk 660041, Russia.
Krasnoyarsk State Med Univ, Res Inst Mol Med & Pathobiochem, P Zheleznyaka 1, Krasnoyarsk 660022, Russia.
Krasnoyarsk State Med Univ, Dept Biochem Med Pharmaceut & Toxicol Chem, P Zheleznyaka 1, Krasnoyarsk 660022, Russia.
Sci Res Inst Med Problems North, P Zheleznyaka 3g, Krasnoyarsk 660022, Russia.
Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Pande, Shubhra; Ranjan, Rajeev; Shuvaev, Anton N.; Malinovskaya, Natalia A.; Ryazanova, Maria; Salmina, Alla B.; Kolenchukova, Oksana A.; Kratasyuk, Valentina A.; Russian Foundation for Basic Research (RFBR)Russian Foundation for Basic Research (RFBR) [16-06-00-439]; Russian Ministry of EducationMinistry of Education and Science, Russian Federation [M 2.2.3]

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16.

Dietary buckwheat enhances sirtuin1 without calorie restriction / S. Pande, R. Ranjan, A. N. Shuvaev [et al.] // J. Cereal Sci. - 2020. - Vol. 94. - Ст. 103004, DOI 10.1016/j.jcs.2020.103004 . - ISSN 0733-5210
Кл.слова (ненормированные):
Calorie restriction -- Dietary buckwheat -- Male wistar rats -- SIRT1 expression
Аннотация: In the present investigation, the role of dietary intervention in male Wistar rats (n = 8, 3 groups) was studied to observe absolute sirtuin 1 (SIRT1) levels (expressed as ng mg?1 total protein) in serum, stomach, liver, and kidney. Dietary buckwheat at 30% (w/w) level of incorporation in the standard diet (Buckwheat Enriched Diet, BED) improved SIRT1 with values 0.933 ± 0.05, 210 ± 7, 63.26 ± 4, and 69.89 ± 3 in serum, stomach, liver, and kidney respectively when compared to the respective control values of 0.536 ± 0.03, 156 ± 23.3, 31.07 ± 2 and 47.11 ± 4. Moreover, BED though isocaloric to CR diet, led to weight gain (g) by 63.11 ± 3.8, ca. 10%, and 40% higher than control (56.27 ± 5.6) and CR (45.05 ± 4.1) diet groups. A marked rise in Feed Efficiency Ratio (FER) by ca. 37% while a 30% decrease in Feed Conversion Ratio (FCR) was observed for the BED group which supports unexpected weight gain in rats post-dietary intervention. The results justify the superior nutritional profile of buckwheat laden with essential nutrients, essential proteins, and bioactives. In contrast, Calorie Restriction (CR) resulted in a decline of the total protein content in circulation by 19%, while reduction of total protein in stomach, liver, and kidney was estimated to be 95%, 35.2%, and 27% respectively though SIRT1 values were comparatively the highest in all the samples studied. A 30-fold enhancement of SIRT1 in stomach post CR is presumed to counter enhanced stress in gastric tissues. Therefore, mild to moderate expression of SIRT1 may confer beneficial effects such as delayed aging and stress resistance but exceedingly high SIRT1 may evoke increased oxidative stress. © 2020 Elsevier Ltd

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, 660041, Russian Federation
Research Institute of Molecular Medicine and Pathobiochemistry, Krasnoyarsk State Medical University Named After Prof. V.F. Voino-Yasenetsky, P. Zheleznyaka 1, Krasnoyarsk, 660022, Russian Federation
Department of Biochemistry, Medical, Pharmaceutical & Toxicological Chemistry, Krasnoyarsk State Medical University Named After Prof. V.F. Voino-Yasenetsky, P. Zheleznyaka 1, Krasnoyarsk, 660022, Russian Federation
Scientific Research Institute of Medical Problems of the North, P. Zheleznyaka 3g, Krasnoyarsk, 660022, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Pande, S.; Ranjan, R.; Shuvaev, A. N.; Malinovskaya, N. A.; Ryazanova, M.; Salmina, A. B.; Kolenchukova, O. A.; Kratasyuk, V. A.

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17.

Effect of different salts and detergents on luciferin-luciferase luminescence of the enchytraeid Fridericia heliota / N. S. Rodionova, V. N. Petushkov // Journal of Photochemistry and Photobiology B: Biology. - 2006. - Vol. 83, Is. 2. - P123-128, DOI 10.1016/j.jphotobiol.2005.12.014 . - ISSN 1011-1344
Кл.слова (ненормированные):
ATP -- Bioluminescence -- Earthworms -- Ions -- Luciferin-luciferase systems -- Triton X-100 -- adenosine triphosphate -- anion -- bromine -- calcium ion -- carbonic acid -- cation -- chloride -- chromium derivative -- detergent -- dodecyl sulfate sodium -- inorganic salt -- iodine -- iron derivative -- luciferase -- luciferin -- magnesium ion -- manganese -- nitrate -- phosphate -- sulfate -- sulfite -- triton x 100 -- annelid worm -- article -- bioluminescence -- concentration (parameters) -- controlled study -- enzyme activation -- enzyme activity -- enzyme inhibition -- enzyme mechanism -- in vitro study -- nonhuman -- priority journal -- qualitative analysis -- quantitative analysis -- Adenosine Triphosphate -- Animals -- Cations, Divalent -- Cations, Monovalent -- Detergents -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescence -- Metals -- Oligochaeta -- Photobiology -- Salts -- Annelida -- Clitellata -- earthworms (sp.) -- Enchytraeidae -- Fridericia heliota -- Oligochaeta (Metazoa) -- Pheretima sieboldi
Аннотация: The study addresses the effect produced by different inorganic salts and detergents (SDS, Triton X-100, the Tween series) on the ATP-dependent bioluminescent reaction catalyzed by the luciferase of the new earthworm species Fridericia heliota (Annelida: Clitellata: Oligochaeta: Enchytraeidae). It has been shown that the effect of divalent metal salts on luminescence is determined by the action of cations. Three of them - Mg2+, Mn2+ and Ca2+ - can stimulate luciferase activity at concentrations varying within a wide range, and Mn2+ can act as a 100%-effective substitute for Mg2+ in F. heliota luminescence reaction in vitro. The inhibitory effect of monovalent metal salts on luminescence is largely determined by the action of the anion part of the molecule. The effectiveness of the inhibitory effect of anions increases in the following order: {Mathematical expression}. Of the sodium salts, dodecyl sulfate, which is an anionic detergent, produces the strongest inhibitory effect on luciferase. On the contrary, nonionic detergents produce a stimulatory effect on the F. heliota luciferase. The action of the most effective of them - Triton X-100 - is determined by its ability to reduce the actual concentration of lipid inhibitors in the reaction mixture. В© 2006 Elsevier B.V. All rights reserved.

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

Доп.точки доступа:
Rodionova, N.S.; Petushkov, V.N.

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18.

Effect of environmental factors on the expression of the catabolite-dependent lux-operon borne by a recombinant plasmid / E. E. Maksimova [et al.] // Microbiology. - 1998. - Vol. 67, Is. 2. - P137-141 . - ISSN 0026-2617
Кл.слова (ненормированные):
Catabolite repression -- Environmental factors -- Escherichia coli -- Introduction into model ecosystems -- Lux-operon -- Recombinant plasmid -- Regulation of expression
Аннотация: Expression of the lux-genes cloned in the recombinant plasmid pPHL7 (Ap1Lux+) 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. В© 1998 MAHK Hayka/Interperiodica Publishing.

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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19.

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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20.

Experimental evaluation of the processes resulting from the introduction of the transgenic microorganism Escherichia coli Z905/pPHL7 (luk(+)) into aquatic microcosms [Text] / T. V. Kargatova [et al.] ; 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. 1769-1774, DOI 10.1016/S0273-1177(03)00119-4. - Cited References: 16 . - ISBN 0273-1177

РУБ Engineering, Aerospace + Astronomy & Astrophysics + Ecology + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences
Рубрики:
SURVIVAL
PROTEIN
Аннотация: The processes resulting from the introduction of the transgenic microorganism (TM) E. coli Z905/pPHL7 into aquatic microcosms have been modeled experimentally. It has been shown that the TM E. coli is able to adapt to a long co-existence with indigenous heterotrophic microflora in variously structured microcosms. In more complex microcosms the numerical dynamics of the introduced E. coli Z905/pPHL7 population is more stable. In the TM populations staying in the microcosms for a prolonged time, changes are recorded in the phenotypic expression of plasmid genes (ampicillin resistance and the luminescence level) and chromosome genes (morphological and physiological traits). However, in our study microcosms, the recombinant plasmid persisted in the TM cells for 6 years after die introduction, and as the population adapts to the conditions of the microcosms, the efficiency of the cloned gene expression in the cells is restored. In the microcosms with high microalgal counts (10(7) cells/ml), cells with a high threshold of sensitivity to ampicillin dominate in the population of the TM E. coli Z905/pPHL7. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

WOS
Держатели документа:
SB RAS, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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