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Формат представления найденных документов:
полный	информационный	краткий

Поисковый запрос: (<.>K=Cnidaria<.>)

Общее количество найденных документов : 1

Recombinant Ca2+-regulated photoproteins of ctenophores: current knowledge and application prospects / L. P. Burakova, E. S. Vysotski // Appl. Microbiol. Biotechnol. - 2019. - Vol. 103, Is. 15. - P5929-5946, DOI 10.1007/s00253-019-09939-0 . - ISSN 0175-7598
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Intracellular calcium -- Photoinactivation -- Absorption spectroscopy -- Alkalinity -- Animals -- Binding sites -- Cloning -- Encoding (symbols) -- Phosphorescence -- Physicochemical properties -- Signal encoding -- Amino acid sequence -- Application prospect -- Biotechnology applications -- Coelenterazine -- Intracellular calcium -- Marine animals -- Photoinactivation -- Structural feature -- Bioluminescence -- Animalia -- Cnidaria -- Ctenophora (coelenterates)
Аннотация: Bright bioluminescence of ctenophores is conditioned by Ca2+-regulated photoproteins. Although they share many properties characteristic of hydromedusan Ca2+-regulated photoproteins responsible for light emission of marine animals belonging to phylum Cnidaria, a substantial distinction still exists. The ctenophore photoproteins appeared to be extremely sensitive to light—they lose the ability for bioluminescence on exposure to light over the entire absorption spectrum. Inactivation is irreversible because keeping the inactivated photoprotein in the dark does not recover its activity. The capability to emit light can be restored only by incubation of inactivated photoprotein with coelenterazine in the dark at alkaline pH in the presence of oxygen. Although these photoproteins were discovered many years ago, only the cloning of cDNAs encoding these unique bioluminescent proteins in the early 2000s has provided a new impetus for their studies. To date, cDNAs encoding Ca2+-regulated photoproteins from four different species of luminous ctenophores have been cloned. The amino acid sequences of ctenophore photoproteins turned out to completely differ from those of hydromedusan photoproteins (identity less than 29%) though also similar to them having three EF-hand Ca2+-binding sites. At the same time, these photoproteins reveal the same two-domain scaffold characteristic of hydromedusan photoproteins. This review is an attempt to systemize and critically evaluate the data scattered through various articles regarding the structural features of recombinant light-sensitive Ca2+-regulated photoproteins of ctenophores and their bioluminescent and physicochemical properties as well as to compare them with those of hydromedusan photoproteins. In addition, we also discuss the prospects of their biotechnology applications. © 2019, Springer-Verlag GmbH Germany, part of Springer Nature.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Vysotski, E. S.

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