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Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state [Text] / G. A. Stepanyuk [et al.] // BBA-Proteins Proteomics. - 2013. - Vol. 1834, Is. 10. - P2139-2146, DOI 10.1016/j.bbapap.2013.07.006. - Cited References: 64. - This work was supported by RFBR grants 09-04-00172, 12-04-00131, 12-04-91153, and NSFC 31270795 and 31021062, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) "Molecular and Cellular Biology" of the RAS. It was also supported in part with funds from the National Institutes of Health (GM62407), The Georgia Research Alliance and the University of Georgia Research Foundation. Data were collected at Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory. Supporting institutions may be found at www.ser-cat.org/members.html. The use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. W-31-109-Eng-38. . - ISSN 1570-9639

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   COELENTERAZINE-BINDING PROTEIN
   CRYSTAL-STRUCTURE
   MNEMIOPSIS-SP
   CA2+-REGULATED PHOTOPROTEINS
   OBELIN BIOLUMINESCENCE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   RENILLA-RENIFORMIS
   APO-OBELIN
Кл.слова (ненормированные):
Coelenterazine -- Calcium -- Bioluminescence -- Luciferase
Аннотация: The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca2+-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0 angstrom. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. (C) 2013 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
[Stepanyuk, Galina A.
Liu, Zhi-Jie
Lee, John
Rose, John
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Burakova, Ludmila P.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
[Liu, Zhi-Jie] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[Liu, Zhi-Jie] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
[Burakova, Ludmila P.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Burakova, L.P.; Lee, J...; Rose, J...; Vysotski, E.S.; Wang, B.C.; RFBR [09-04-00172, 12-04-00131, 12-04-91153]; NSFC [31270795, 31021062]; Government of Russian Federation of the RAS [11.G34.31.0058]; National Institutes of Health [GM62407]; Georgia Research Alliance; University of Georgia Research Foundation; U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]

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The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein / S. V. Markova [et al.] // FEBS J. - 2012. - Vol. 279, Is. 5. - P856-870, DOI 10.1111/j.1742-4658.2012.08476.x. - Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany). . - ISSN 1742-464X

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   C-TERMINAL PROLINE
   SEQUENCE-ANALYSIS
   MNEMIOPSIS-SP
   COELENTERAZINE-BINDING
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURES
   EXCITED-STATE
   CDNA CLONING
Кл.слова (ненормированные):
bioluminescence -- calcium -- coelenterazine -- luciferase -- mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Malikova, Natalia P.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Dept Biophys, Krasnoyarsk, Russia
[Golz, Stefan] Bayer Pharma AG, Global Drug Discovery, Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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