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Aliidiomarina shirensis sp nov., a halophilic bacterium isolated from Shira Lake in Khakasia, southern Siberia, and a proposal to transfer Idiomarina maris to the genus Aliidiomarina [Text] / H. H. Chiu [et al.] // Int. J. Syst. Evol. Microbiol. - 2014. - Vol. 64. - P1334-1339, DOI 10.1099/ijs.0.057851-0. - Cited References: 22. - We thank Dr Egor S. Zadereev and Dr Vladimir V. Zykov at the Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk, for assistance with sampling. This study was supported by Russia Taiwan joint project funding (NSC 99-2923-B-001-001-MY3) from the National Science Council, Taiwan, the Russian Foundation for Basic Research, Grant No. 14-04-01060-a and Siberian Branch of Russian Academy of Sciences, joint Taiwan-Siberian Project No. 11. . - ISSN 1466-5026. - ISSN 1466-5034

РУБ Microbiology
Рубрики:
SHALLOW COASTAL WATER
   RIBOSOMAL-RNA GENE
   EMENDED DESCRIPTION
   PSEUDIDIOMARINA
   PHYLOTYPES
   SEQUENCE
   TAIWAN
Аннотация: Strain AIS(T), an aerobic halophilic, Gram-reaction-negative, heterotrophic bacterium isolated from the water of Shira Lake in Khakasia, southern Siberia, was characterized using a polyphasic approach. Our analysis of the 16S rRNA gene sequences showed that 'Aliidiomarina haloalkalitolerans', 'Allidiomarina sanyensis', Idiomarina maris and AIS(T) formed a distinct lineage. The sequence similarities between AIS(T) and the type strains of species of the genera Idiomarina and Aliidiomarina were 91.6-95.1 % and 94.0-96.9 %, respectively. The major isoprenoid quinone of AIS(T) was ubiquinone 8 (Q-8). Predominant cellular fatty acids were iso-C-17:0, iso-C-15:0 and summed feature 9. The genomic DNA G+C content was 45.8 mol%. It is concluded that AIS(T) represents a novel species of the genus Aliidiomarina, and the name Aliidiomarina shirensis sp. nov. is herein proposed for it. The type strain is AIST (=JCM 17761(T)=BCRC 80327(T)). Based on its fatty acid profile and our phylogenetic analysis, we propose that Idiomarina mans be transferred to the genus Aliidiomarina.

WOS
Держатели документа:
[Chiu, Hsiu-Hui
Tang, Sen-Lin] Acad Sinica, Biodivers Res Ctr, Taipei 115, Taiwan
[Rogozin, Denis Yu.
Degermendzhy, Andrei G.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Rogozin, Denis Yu.] Siberian Fed Univ, Krasnoyarsk, Russia
[Huang, Ssu-Po
Shieh, Wung Yang] Natl Taiwan Univ, Inst Oceanog, Taipei 10764, Taiwan
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Chiu, H.H.; Rogozin, D.Y.; Huang, S.P.; Degermendzhy, A.G.; Shieh, W.Y.; Tang, S.L.; National Science Council, Taiwan [NSC 99-2923-B-001-001-MY3]; Russian Foundation for Basic Research [14-04-01060-a]; Siberian Branch of Russian Academy of Sciences, joint Taiwan-Siberian Project [11]

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Crystal structure of a Ca2+-discharged photoprotein - Implications for mechanisms of the calcium trigger and bioluminescence [Text] / L. . Deng [et al.] // J. Biol. Chem. - 2004. - Vol. 279, Is. 32. - P33647-33652, DOI 10.1074/jbc.M402427200. - Cited References: 31 . - ISSN 0021-9258

РУБ Biochemistry & Molecular Biology
Рубрики:
VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   ELECTRON-DENSITY
   W92F OBELIN
   AEQUORIN
   PROTEINS
   LIGHT
   SEQUENCE
   BINDING
   COELENTERAZINE
Аннотация: Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigger and for generation of the different excited states that are the origin of the different colors of bioluminescence. Here we report the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-Angstrom resolution. The results lend support to the proposed mechanisms and provide new structural insight into details of these processes. Global conformational changes caused by Ca2+ association are typical of the class of calcium signal modulators within the EF-hand protein superfamily. Accommodation of the Ca2+ ions into the loops of the EF-hands is seen to propagate into the active site of the protein now occupied by the coelenteramide where there is a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis. Also the H-bonding between His-22 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of coelenteramide, confirming the proposed rapid excited state proton transfer that would lead to the excited state of the phenolate ion pair, which is responsible for the blue emission of bioluminescence.

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...; Markova, S.V.; Vysotski, E.S.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN [Текст] / Y. S. VYSOTSKII, V. S. BONDAR, I. I. GITELZON // DOKLADY AKADEMII NAUK SSSR. - 1991. - Vol. 321, Is. 1. - С. 214-217. - Cited References: 14 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   BEROE-OVATA
   AEQUORIN
   PROTEIN
   PURIFICATION
   EXTRACTION
   PHIALIDIN
   SEQUENCE
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
VYSOTSKII, Y.S.; BONDAR, V.S.; GITELZON, I.I.

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Model of the active site of firefly luciferase [Text] / T. P. Sandalova, N. N. Ugarova // Biochem.-Moscow. - 1999. - Vol. 64, Is. 8. - P. 962-967. - Cited References: 20 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
ESCHERICHIA-COLI
   SEQUENCE
   CLONING
   ENZYME
   CDNA
   SUPERFAMILY
Кл.слова (ненормированные):
bioluminescence -- firefly luciferase -- ATP -- luciferin -- spatial structure -- active site -- enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Karolinska Inst, S-17177 Stockholm, Sweden
Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sandalova, T.P.; Ugarova, N.N.

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Preparation and X-ray crystallographic analysis of the Ca2+-discharged photoprotein obelin [Text] / L. . Deng [et al.] // Acta Crystallogr. Sect. D-Biol. Crystallogr. - 2004. - Vol. 60. - P512-514, DOI 10.1107/S090744490302852X. - Cited References: 18 . - ISSN 0907-4449

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Biophysics + Crystallography
Рубрики:
VIOLET BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   W92F OBELIN
   AEQUORIN
   SEQUENCE
   PROTEIN
   CLONING
   CDNA
Аннотация: Ca2+-regulated photoproteins belong to the EF-hand Ca2+-binding protein family. The addition of calcium ions initiates bright blue bioluminescence of the photoproteins, a result of the oxidative breakdown of coelenterazine peroxide to coelenteramide. Crystals of the Ca2+-discharged W92F mutant of obelin from Obelia longissima have been grown, representing the first crystallization of a photoprotein after the Ca2+-triggered bioluminescence. A green fluorescence observed from the crystals clearly demonstrates that coelenteramide, the bioluminescence product of coelenterazine peroxide, is bound within the protein. The diffraction pattern exhibits tetragonal Laue symmetry. Systematic absences indicate that the space group is either P4(3)2(1)2 or P4(1)2(1)2. The unit-cell parameters are a=b=53.4, c=144.0 Angstrom. The crystals diffract to 1.9 Angstrom resolution.

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...; Markova, S.V.; Vysotski, E.S.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin [Text] / V. S. Bondar [et al.] // Biochem.-Moscow. - 2001. - Vol. 66, Is. 9. - P1014-1018, DOI 10.1023/A:1012377827626. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CDNA
   EXPRESSION
   AEQUORIN
   SEQUENCE
   CLONING
Кл.слова (ненормированные):
photoproteins -- obelin -- apoobelin mutants -- bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein > S-mutant > A-mutant. This is consistent with rank of nucleophilicity SH > OH > CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.

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:
Bondar, V.S.; Purtov, K.V.; Malikova, N.P.; Frank, L.A.; Illarionov, B.A.

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