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All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

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Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
Свободных экз. нет
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Transient-state kinetic analysis of complex formation between photoprotein clytin and GFP from jellyfish Clytia gregaria [Text] / E. V. Eremeeva, E. S. van Berkel, E. S. Vysotski // FEBS Lett. - 2016. - Vol. 590, Is. 3. - P307-316, DOI 10.1002/1873-3468.12052. - Cited References:34. - This study was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0014-5793. - ISSN 1873-3468

РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
GREEN-FLUORESCENT PROTEIN
ENERGY-TRANSFER
CA2+-REGULATED
Кл.слова (ненормированные):
aequorin -- bioluminescence -- coelenterazine -- FRET -- obelin -- protein-protein -- interaction
Аннотация: Luminous organisms use different protein-mediated strategies to modulate light emission color. Here, we report the transient-state kinetic studies of the interaction between photoprotein clytin from Clytia gregaria and its antenna protein, cgreGFP. We propose that cgreGFP forms a transient complex with Ca2+-bound clytin before the excited singlet state of the coelenteramide product is formed. From the spectral distribution and donor-acceptor separation distance, we infer that clytin reaction intermediates may interact only with the middle side part of cgreGFP.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Wageningen Univ, Biochem Lab, NL-6700 AP Wageningen, Netherlands.

Доп.точки доступа:
Eremeeva, Elena V.; van Berkel, Willem J. H.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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Creation of Artificial Luciferases to Expand their Analytical Potential [Text] / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929, DOI 10.2174/1386207318666150917100011. - Cited References:79. - The work was supported by: the RFBR grant No. 14-08-00902/14; the State budget allocated to the fundamental research at the Russian Academy of Sciences (project No. VI 57.1.1). . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
BIOLUMINESCENT REPORTER APPLICATIONS
COELENTERAZINE-BINDING PROTEIN
Кл.слова (ненормированные):
Luciferase -- luciferin -- photoprotein -- bioluminescence -- mutagenesis -- luciferase-based assay -- bioimaging -- reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescence-based analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Frank, Ludmila A.; RFBR [14-08-00902/14]; [VI 57.1.1]

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Semisynthetic photoprotein reporters for tracking fast Ca2+ transients / N. P. Malikova, A. J. Borgdorff, E. S. Vysotski // Photochem. Photobiol. Sci. - 2015. - Vol. 14, Is. 12. - P2213-2224, DOI 10.1039/c5pp00328h . - ISSN 1474-905X
Аннотация: Changes in the intracellular concentration of free ionized calcium ([Ca2+]i) control a host of cellular processes as varied as vision, muscle contraction, neuronal signal transmission, proliferation, apoptosis etc. The disturbance in Ca2+-signaling causes many severe diseases. To understand the mechanisms underlying the control by calcium and how disorder of this regulation relates to pathological conditions, it is necessary to measure [Ca2+]i. The Ca2+-regulated photoproteins which are responsible for bioluminescence of marine coelenterates have been successfully used for this purpose over the years. Here we report the results on comparative characterization of bioluminescence properties of aequorin from Aequorea Victoria, obelin from Obelia longissima, and clytin from Clytia gregaria charged by native coelenterazine and coelenterazine analogues f, i, and hcp. The comparison of specific bioluminescence activity, stability, emission spectra, stopped-flow kinetics, sensitivity to calcium, and effect of physiological concentrations of Mg2+ establishes obelin-hcp as an excellent semisynthetic photoprotein to keep track of fast intracellular Ca2+ transients. The rate of rise of its light signal on a sudden change of [Ca2+] is almost 3- and 11-fold higher than those of obelin and aequorin with native coelenterazine, respectively, and 20 times higher than that of the corresponding aequorin-hcp. In addition, obelin-hcp preserves a high specific bioluminescence activity and displays higher Ca2+-sensitivity as compared to obelin charged by native coelenterazine and sensitivity to Ca2+ comparable with those of aequorin-f and aequorin-hcp. © The Royal Society of Chemistry and Owner Societies 2015.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Institut des Neurosciences Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique, Avenue de la Terrasse, Gif-sur-Yvette, France

Доп.точки доступа:
Malikova, N. P.; Borgdorff, A. J.; Vysotski, E. S.
Свободных экз. нет
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Creation of artificial luciferases to expand their analytical potential / L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P919-929 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioimaging -- Bioluminescence -- Luciferase -- Luciferase-based assay -- Luciferin -- Mutagenesis -- Photoprotein -- Reporter assay
Аннотация: Bioluminescent proteins have been intensively used as high sensitive reporters in all kinds of binding assays (immuno-, nucleic acid hybridization assays, etc.) and in bioimaging. But natural luciferases do not always meet the requirements set for them as the assay reporters: thermostabitity, definite bioluminescence spectral and kinetics characteristics, stability to chemical modifications, etc. Luciferases with different appropriate characteristics as well as various luciferin derivatives were obtained using mutagenesis and chemical synthesis. Thanks to rigorous efforts of many researchers bioluminescencebased analytical techniques offer a great potential for solving analytical tasks in the field of biotechnology, biomedicine, pharmacology, etc. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnii ave., 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Frank, L. A.

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On the mechanism of biological activation by tritium / T. V. Rozhko [et al.] // J. Environ. Radioact. - 2016. - Vol. 157. - P131-135, DOI 10.1016/j.jenvrad.2016.03.017 . - ISSN 0265-931X
Кл.слова (ненормированные):
DNA mutations -- Low-dose effect -- Luminous marine bacteria -- Radiation hormesis -- Tritium
Аннотация: The mechanism of biological activation by beta-emitting radionuclide tritium was studied. Luminous marine bacteria were used as a bioassay to monitor the biological effect of tritium with luminescence intensity as the physiological parameter tested. Two different types of tritium sources were used: HTO molecules distributed regularly in the surrounding aqueous medium, and a solid source with tritium atoms fixed on its surface (tritium-labeled films, 0.11, 0.28, 0.91, and 2.36 MBq/cm2). When using the tritium-labeled films, tritium penetration into the cells was prevented. The both types of tritium sources revealed similar changes in the bacterial luminescence kinetics: a delay period followed by bioluminescence activation. No monotonic dependences of bioluminescence activation efficiency on specific radioactivities of the films were found. A 15-day exposure to tritiated water (100 MBq/L) did not reveal mutations in bacterial DNA. The results obtained give preference to a "non-genomic" mechanism of bioluminescence activation by tritium. An activation of the intracellular bioluminescence process develops without penetration of tritium atoms into the cells and can be caused by intensification of trans-membrane cellular processes stimulated by ionization and radiolysis of aqueous media. © 2016 Elsevier Ltd.

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Держатели документа:
Krasnoyarsk State Medical Academy, P.Zheleznyaka 1, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny 79, Krasnoyarsk, Russian Federation
Moscow State University, Department of Chemistry, Moscow, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Rozhko, T. V.; Badun, G. A.; Razzhivina, I. A.; Guseynov, O. A.; Guseynova, V. E.; Kudryasheva, N. S.

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Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin / L. P. Burakova [et al.] // Photochem. Photobiol. Sci. - 2016. - Vol. 15, Is. 5. - P691-704, DOI 10.1039/c6pp00050a . - ISSN 1474-905X
Аннотация: Bright bioluminescence of ctenophores is caused by Ca2+-regulated photoproteins. Although these photoproteins are functionally identical to and share many properties of cnidarian photoproteins, like aequorin and obelin, and retain the same spatial architecture, they are extremely sensitive to light, i.e. lose the ability to bioluminesce on exposure to light over the entire absorption spectrum. In addition, the degree of identity of their amino acid sequences with those of cnidarian photoproteins is only 29.4%. This suggests that the residues involved in bioluminescence of ctenophore and cnidarian photoproteins significantly differ. Here we describe the bioluminescent properties of berovin mutants with substitution of the residues located in the photoprotein internal cavity. Since the spatial structure of berovin bound with a substrate is not determined yet, to identify these residues we have modeled it with an accommodated substrate using the structures of some cnidarian Ca2+-regulated photoproteins with bound coelenterazine or coelenteramide as templates in order to obtain an adequate sampling and to take into account all possible conformers and variants for ligand-protein docking. Based on the impact of substitutions on the bioluminescent properties and model structures we speculate that within the internal cavity of ctenophore photoproteins, coelenterazine is bound as a 2-peroxy anion adduct which is stabilized owing to Coulomb interaction with a positively charged guanidinium group of Arg41 paired with Tyr204. In this case, the bioluminescence reaction is triggered by only calcium-induced conformational changes leading to the disturbance of charge-charge interaction. © 2016 The Royal Society of Chemistry and Owner Societies.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Stepanyuk, G. A.; Eremeeva, E. V.; Vysotski, E. S.

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Simultaneous genotyping of four single nucleotide polymorphisms associated with risk factors of hemostasis disorders / E. E. Bashmakova, V. V. Krasitskaya, L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P930-936 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescent microassay -- Multiplex PCR -- PEXT reaction -- Photoprotein obelin -- SNP detection
Аннотация: Multiplex simultaneous genotyping technique was developed for four polymorphisms in genes coding for blood coagulation factors and homocysteine metabolism which are considered as thrombophilia related mutations: FV Leiden, FII G20210A, MTHFR C677T, and FVII G10976A. It is based on primer extension reaction with the following bioluminescent solid-phase microassay. At that, two different in bioluminescence obelin mutants were applied to simultaneous detection of two gene allelic variants. The assay is carried out in microtiter plate format and provides fast and reliable genotyping of four single nucleotide polymorphisms in four different genes within 2.5 hours. A large number of clinical samples were analyzed and the obtained results were found to be in complete correlation with those obtained by using conventional RT-PCR techniques. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Bashmakova, E. E.; Krasitskaya, V. V.; Frank, L. A.

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Applications of luminous bacteria enzymes in toxicology / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescence -- Bioluminescent toxicity enzymatic assay -- Immobilization of enzymes -- Luciferase -- Total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation
Photobiology Laboratory, Russian Academy of Sciences, Siberian Branch, Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kratasyuk, V. A.; Esimbekova, E. N.

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10.

Applications of Luminous Bacteria Enzymes in Toxicology [Text] / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959, DOI 10.2174/1386207318666150917100257. - Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Кл.слова (ненормированные):
Bioluminescence -- bioluminescent toxicity enzymatic assay -- immobilization -- of enzymes -- luciferase -- total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH: FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Esimbekova, Elena N.; Russian Science Foundation [15-19-10041]

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11.

Impact of enzyme stabilizers on the characteristics of biomodules for bioluminescent biosensors / V. Lonshakova-Mukina, E. Esimbekova, V. Kratasyuk // Sens Actuators, B Chem. - 2015. - Vol. 213. - P244-247, DOI 10.1016/j.snb.2015.02.061 . - ISSN 0925-4005
Кл.слова (ненормированные):
Bioluminescence -- Body fluids -- Carrier concentration -- Enzymes -- Starch -- Bioluminescent biosensor -- Bovine serum albumins -- Dithiothreitol -- Maximum permissible concentration -- Mercaptoethanol -- Oxidoreductases -- Storage stability -- Toxic substances -- Biosensors
Аннотация: The biomodule of bioluminescent biosensor based on a coupled enzyme system NADH:FMN-oxidoreductase and luciferase, co-immobilized with substrates in dried starch or gelatin gels, has been developed. We studied the impact of several stabilizers - dithiothreitol (DTT), bovine serum albumin (BSA) and mercaptoethanol (ME) on the biomodule's activity, storage stability and sensitivity to toxic substances. The inclusion of stabilizers increases the activity of the biological module by more than 150%. To achieve the combination of high activity, prolonged storage time and acute sensitivity to toxic substances within maximum permissible concentration we used starch gel as a carrier adding 100 ?M DTT to the immobilized preparation. The gelatin-based biological module had greater storage stability than the starch-based one but demonstrated less sensitivity to toxic substances. © 2015 Elsevier B.V. All rights reserved.

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Держатели документа:
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50Krasnoyarsk, Russian Federation
ИБФ СО РАН

Доп.точки доступа:
Lonshakova-Mukina, V.; Esimbekova, E.; Kratasyuk, V.

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12.

Novel Mechanism of Bioluminescence: Oxidative Decarboxylation of a Moiety Adjacent to the Light Emitter of Fridericia Luciferin [Text] / M. A. Dubinnyi [et al.] // Angew. Chem.-Int. Edit. - 2015. - Vol. 54, Is. 24. - P7065-7067, DOI 10.1002/anie.201501668. - Cited References:15. - We thank Dr. K.V. Antonov for acquisition of LC-HRMS spectra and Prof. Gary Schuster for fruitful discussion. This work was supported by the Russian Science Foundation grant 14-50-00131. M.S.B. acknowledges support by a stipend program of the President of the Russian Federation. K.M.S. acknowledges generous support from the National Science Foundation (CHE-1213047). This research was carried out using the equipment provided by IBCH core facility (CKP IBCH). . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
CHEMILUMINESCENCE
CYPRIDINA
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- luciferin -- oxidative -- decarboxylation -- peptides
Аннотация: A novel luciferin from a bioluminescent Siberian earthworm Fridericia heliota was recently described. In this study, the Fridericia oxyluciferin was isolated and its structure elucidated. The results provide insight into a novel bioluminescence mechanism in nature. Oxidative decarboxylation of a lysine fragment of the luciferin supplies energy for light generation, while a fluorescent CompX moiety remains intact and serves as the light emitter.

WOS
Держатели документа:
Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia.
Pirogov Russian Natl Res Med Univ, Moscow 117997, Russia.
Russian Acad Sci, Akademgorodok, Siberian Branch, Lab Photobiol,Inst Biophys, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Branch Shemyakin, Pushchino 142290, Russia.
Russian Acad Sci, Ovchinnikov Inst Bioorgan Chem, Pushchino 142290, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Baranov, Mikhail S.; Gorokhovatsky, Andrey Yu.; Kotlobay, Alexey; Solntsev, Kyril M.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]; President of the Russian Federation; National Science Foundation [CHE-1213047]

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13.

The smallest natural high-active luciferase: Cloning and characterization of novel 16.5-kDa luciferase from copepod Metridia longa [Text] / S. V. Markova [et al.] // Biochem. Biophys. Res. Commun. - 2015. - Vol. 457, Is. 1. - P77-82, DOI 10.1016/j.bbrc.2014.12.082. - Cited References:20. - The cloning of cDNA encoding MLuc7 luciferase of M. longa was supported by Bayer AG (Germany); all other studies - by the grant 14-14-01119 of the Russian Science Foundation. We declare that authors have no conflict of interest. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
   SECRETED LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Mammalian -- expression -- Real-time imaging
Аннотация: Coelenterazine-dependent copepod luciferases containing natural signal peptide for secretion are a very convenient analytical tool as they enable monitoring of intracellular events with high sensitivity, without destroying cells or tissues. This property is well suited for application in biomedical research and development of cell-based assays for high throughput screening. We report the cloning of cDNA gene encoding a novel secreted non-allelic 16.5-kDa isoform (MLuc7) of Metridia longa luciferase, which, in fact, is the smallest natural luciferase of known for today. Despite the small size, isoform contains 10 conservative Cys residues suggesting the presence of up to 5 S-S bonds. This hampers the efficient production of functionally active recombinant luciferase in bacterial expression systems. With the use of the baculovirus expression system, we produced substantial amounts of the proper folded MLuc7 luciferase with a yield of similar to 3 mg/L of a high purity protein. We demonstrate that MLuc7 produced in insect cells is highly active and extremely thermostable, and is well suited as a secreted reporter when expressed in mammalian cells ensuring higher sensitivity of detection as compared to another Metridia luciferase isoform (MLuc164) which is widely employed in real-time imaging. (C) 2014 Elsevier Inc. All rights reserved.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.
ИБФ СО РАН

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Burakova, Ludmila P.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Science Foundation [14-14-01119]

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14.

Novel Peptide Chemistry in Terrestrial Animals: Natural Luciferin Analogues from the Bioluminescent Earthworm Fridericia heliota [Text] / M. A. Dubinnyi [et al.] // Chem.-Eur. J. - 2015. - Vol. 21, Is. 10. - P3942-3947, DOI 10.1002/chem.201406498. - Cited References:17. - We thank Dr. K. V. Antonov for registration of LC-HRMS spectra. This work was supported by the Russian Science Foundation grant 14-50-00131. . - ISSN 0947-6539. - ISSN 1521-3765

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
DERIVATIVES
IDENTIFICATION
Кл.слова (ненормированные):
bioluminescence -- Fridericia heliota -- luciferin -- peptides -- structure -- elucidation
Аннотация: We report isolation and structure elucidation of AsLn5, AsLn7, AsLn11 and AsLn12: novel luciferin analogs from the bioluminescent earthworm Fridericia heliota. They were found to be highly unusual modified peptides, comprising either of the two tyrosine-derived chromophores, CompX or CompY and a set of amino acids, including threonine, gamma-aminobutyric acid, homoarginine, and unsymmetrical N,N-dimethylarginine. These natural compounds represent a unique peptide chemistry found in terrestrial animals and rise novel questions concerning their biosynthetic origin.

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Scopus
Держатели документа:
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation
Laboratory of Photobiology, Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Dubinnyi, Maxim A.; Tsarkova, Aleksandra S.; Petushkov, Valentin N.; Kaskova, Zinaida M.; Rodionova, Natalja S.; Kovalchuk, Sergey I.; Ziganshin, Rustam H.; Baranov, Mikhail S.; Mineev, Konstantin S.; Yampolsky, Ilia V.; Russian Science Foundation [14-50-00131]

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15.

The Chemical Basis of Fungal Bioluminescence / K. V. Purtov [et al.] // Angew. Chem. Int. Ed. - 2015. - Vol. 54, Is. 28. - P8124-8128, DOI 10.1002/anie.201501779 . - ISSN 1433-7851
Кл.слова (ненормированные):
bioluminescence -- bioorganic chemistry -- biosynthesis -- luciferin -- natural products -- Biochemistry -- Bioluminescence -- Biosynthesis -- Metabolites -- Phosphorescence -- Biochemical mechanisms -- Bioorganic chemistry -- luciferin -- Natural products -- Plant secondary metabolites -- Structural similarity -- Fungi
Аннотация: Many species of fungi naturally produce light, a phenomenon known as bioluminescence, however, the fungal substrates used in the chemical reactions that produce light have not been reported. We identified the fungal compound luciferin 3-hydroxyhispidin, which is biosynthesized by oxidation of the precursor hispidin, a known fungal and plant secondary metabolite. The fungal luciferin does not share structural similarity with the other eight known luciferins. Furthermore, it was shown that 3-hydroxyhispidin leads to bioluminescence in extracts from four diverse genera of luminous fungi, thus suggesting a common biochemical mechanism for fungal bioluminescence. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Держатели документа:
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation
Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, Moscow, Russian Federation
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan
Pirogov Russian National Research Medical University, Ostrovitianov 1, Moscow, Russian Federation

Доп.точки доступа:
Purtov, K.V.; Petushkov, V.N.; Baranov, M.S.; Mineev, K.S.; Rodionova, N.S.; Kaskova, Z.M.; Tsarkova, A.S.; Petunin, A.I.; Bondar, V.S.; Rodicheva, E.K.; Medvedeva, S.E.; Oba, Y.; Arseniev, A.S.; Lukyanov, S.; Gitelson, J.I.; Yampolsky, I.V.

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16.

Growth and light emission of luminous basidiomycetes cultivated on solid media and in submerged culture [Text] / S. E. Medvedeva [et al.] // Mycosphere. - 2014. - Vol. 5, Is. 4. - P565-577, DOI 10.5943/mycosphere/5/4/9. - Cited References:23. - This study was supported by grant No. 11.G34.31.058 (RF Government) and Projects No. 71 and No. 38 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
MYCELIAL GROWTH
   PANELLUS-STYPTICUS
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
luminescence -- luminous higher fungi -- mycelium
Аннотация: There are higher fungi that emit visible light; however, little is known about their requirements for good growth and bright luminescence. Knowledge of these requirements is extremely important for maintaining fungal cultures in laboratory conditions and preparation of luminous mycelia for research purposes. Luminous higher fungi Panellus stipticus, Armillaria sp. and Neonothopanus nambi isolated from different climatic areas and maintained in CCIBSO 836 (Collection of IBP SB RAS, Russia) were used for experiments. Techniques for static and submerged cultivation of mycelia of higher fungi have been developed and optimized for the production of samples of aerial and globular mycelia with prolonged and stable luminescence. We investigated the growth characteristics and luminescence of mycelia cultivated in/on different nutrient media, and the effects of deionized water and mechanical damage on the light emission of mycelia. An increase in luminescence intensity of fungal mycelia can be obtained during cultivation of fungi on a nutrient medium with a certain composition. A significant increase in light emission from N. nambi mycelium can also be obtained after its incubation in water and mechanical damage. The light emission from N. nambi mycelium was greatly enhanced after these treatments, in contrast to the mycelia of Armillaria sp. or P. stipticus. Cultivation conditions that enable growing mycelia with high levels of luminescence will expedite further studies to gain a better understanding of fungal bioluminescence.

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Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Medvedeva, S. E.; Artemenko, K. S.; Krivosheenko, A. A.; Rusinova, A. G.; Rodicheva, E. K.; Puzyr, A. P.; Bondar, V. S.; RF Government [11.G34.31.058]; SB RAS [71, 38]

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17.

Simultaneous Genotyping of Four Single Nucleotide Polymorphisms Associated with Risk Factors of Hemostasis Disorders [Text] / E. E. Bashmakova, V. V. Krasitskaya, L. A. Frank // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P930-936, DOI 10.2174/1386207318666150917095903. - Cited References:20. - The study was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
ALLELE-SPECIFIC PCR
FACTOR-V-LEIDEN
BIOLUMINESCENT IMMUNOASSAY
Кл.слова (ненормированные):
SNP detection -- PEXT reaction -- photoprotein obelin -- bioluminescent -- microassay -- multiplex PCR
Аннотация: Multiplex simultaneous genotyping technique was developed for four polymorphisms in genes coding for blood coagulation factors and homocysteine metabolism which are considered as thrombophilia related mutations: FV Leiden, FII G20210A, MTHFR C677T, and FVII G10976A. It is based on primer extension reaction with the following bioluminescent solid-phase microassay. At that, two different in bioluminescence obelin mutants were applied to simultaneous detection of two gene allelic variants. The assay is carried out in microtiter plate format and provides fast and reliable genotyping of four single nucleotide polymorphisms in four different genes within 2.5 hours. A large number of clinical samples were analyzed and the obtained results were found to be in complete correlation with those obtained by using conventional RT-PCR techniques.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Krasitskaya, Vasilisa V.; Frank, Ludmila A.; Russian Science Foundation [14-14-01119]

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18.

Coelenterazine-dependent luciferases / S. V. Markova, E. S. Vysotski // Biochemistry Moscow. - 2015. - Vol. 80, Is. 6. - P714-732, DOI 10.1134/S0006297915060073 . - ISSN 0006-2979
Кл.слова (ненормированные):
bioluminescence -- coelenterazine -- luciferase -- luciferin -- Coelenterata -- Cypridina luciferin -- Fungi -- Hexapoda -- Mollusca -- Protozoa
Аннотация: Bioluminescence is a widespread natural phenomenon. Luminous organisms are found among bacteria, fungi, protozoa, coelenterates, worms, molluscs, insects, and fish. Studies on bioluminescent systems of various organisms have revealed an interesting feature - the mechanisms underlying visible light emission are considerably different in representatives of different taxa despite the same final result of this biochemical process. Among the several substrates of bioluminescent reactions identified in marine luminous organisms, the most commonly used are imidazopyrazinone derivatives such as coelenterazine and Cypridina luciferin. Although the substrate used is the same, bioluminescent proteins that catalyze light emitting reactions in taxonomically remote luminous organisms do not show similarity either in amino acid sequences or in spatial structures. In this review, we consider luciferases of various luminous organisms that use coelenterazine or Cypridina luciferin as a substrate, as well as modifications of these proteins that improve their physicochemical and bioluminescent properties and therefore their applicability in bioluminescence imaging in vivo. © 2015 Pleiades Publishing, Ltd.

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Держатели документа:
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk, Russian Federation

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

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19.

Total peroxidase and catalase activity of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in comparison with the level of light emission [Text] / O. A. Mogil'naya [et al.] // Appl. Biochem. Microbiol. - 2015. - Vol. 51, Is. 4. - P419-424, DOI 10.1134/S0003683815040110. - Cited References:35. - The authors are grateful to N. V. Psurtseva (curator of the collection of basidiomycetes of the Botanical Institute, Russian Academy of Science) for help with the species affiliation of the IBSO 2328 culture. This work was supported by the Program of Interdisciplinary Projects of the Siberian Branch of the Russian Academy of Sciences, project no. 71. . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
OXIDATIVE STRESS
   SYSTEM
   FUNGI
   BIOLUMINESCENCE
   LUMINESCENCE
Кл.слова (ненормированные):
basidiomycetes -- luminescence -- peroxidase -- catalase
Аннотация: The peroxidase and catalase activities in the mycelium of luminous basidiomycetes Armillaria borealis and Neonothopanus nambi in normal conditions and under stress were compared. An increase in the luminescence level was observed under stress, as well as an increase in peroxidase and catalase activities. Moreover, the peroxidase activity in extracts of A. borealis mycelium was found to be almost one and a half orders of magnitude lower, and the catalase activity more than two orders of magnitude higher in comparison with the N. nambi mycelium. It can be suggested that the difference between the brightly luminescent and dimly luminescent mycelium of N. nambi is due to the content of (HO2)-O-2 or other peroxide compounds.

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Scopus
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogil'naya, O. A.; Ronzhin, N. O.; Medvedeva, S. E.; Bondar', V. S.; Siberian Branch of the Russian Academy of Sciences [71]

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20.

The use of glowing wood as a source of luminescent culture of fungus mycelium [Text] / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2016. - Vol. 7, Is. 1. - P1-17, DOI 10.5943/mycosphere/7/1/1. - Cited References:22. - The authors are grateful to Prof. A. Frank, Director of North Borneo Biostation, for the opportunity to carry out studies of glowing wood; to Nadezhda N. Kudashova, a senior researcher at the Institute of Biology and Biophysics at the Tomsk University, for identifying the species of nonluminous fungi. This study was supported by grant no. 11.G34.31.0058 (RF Government) and Projects no. 71 (SB RAS). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
BIOLUMINESCENCE CHARACTERISTICS
NEONOTHOPANUS-NAMBI
LIGHT-EMISSION
Кл.слова (ненормированные):
Bioluminescence -- culture of luminous mycelia -- kinetics of luminescent -- reaction -- light emitting wood -- luminous fungus
Аннотация: In studies of fungal bioluminescence, not only fruiting bodies and spores of the fungus, but also samples of luminescent wood, leaf litter or soil may need to be used to derive pure mycelial culture. This study describes an approach to isolating the culture of luminescent fungal mycelium from samples of light-emitting wood found on Borneo Island in November-December 2013. A GelDoc XR Imaging System (Bio-Rad Laboratories, Inc., U.S.) was used for the first time to monitor luminescence and select luminous samples. This study shows that for successful isolation of the culture of luminescent mycelium out of the luminescent wood found in the forest, it is imperative to keep the samples moist (mycelium alive until there is water), while immediate and aseptic delivery of the samples to the laboratory is not a crucial condition (inner layers of wood is "sterile"). Investigation of the growth features of the isolated mycelium in various growing conditions revealed some peculiar properties of its luminescence in comparison with the known luminescent cultures of basidiomycetes. When grown on solid nutrient media, mycelium exhibits low growth rates, long-lasting luminescence (140 days or longer), and emergence and disappearance of local zones with high levels of light emission. Mycelium produced in submerged culture does not emit light, and this effect must be caused by the absence or a very low level of the luminescent reaction substrate in the biomass. The luminescence system isolated from mycelial biomass did not induce luminescent reaction in vitro upon the addition of NADPH (recording intensity is 60 100 URL/sec). We found that enzymes of the luminescence systems isolated from mycelium pellets retained their activity and catalyzed luminescent reaction when a hot extract of the luminous fungus Armillaria sp. (IBSO 2360) was added (near 1900 URL/sec). The same effect was obtained after addition of hot extracts from the fruiting bodies of nonluminous higher fungi Pholiota squarrosa, Cortinarius sp., Hypholoma capnoides and Chroogomphus rutilus (near 3500 URL/sec). The pure culture of luminescent mycelium has been registered in the Culture Collection of IBP SB RAS as IBSO 2371; now it can be used for various in vivo and in vitro studies, including identification of the fungus.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Bondar, V. S.; RF Government [11.G34.31.0058]; SB RAS [71]

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