The unique protein-to-protein carotenoid transfer mechanism

Maksimov, E.G.; Sluchanko, N.N.; Slonimskiy, Y.B.; Mironov, K.S.; Klementiev, K.E.; Goryachev, S.N.; Marcus, M.; Thomas, F.; Los, D.A.; Paschenko, V.Z.; Rubin, A.B.

Авторы: Maksimov Eugene G., Sluchanko Nikolai N., Slonimskiy Yuri B., Mironov Kirill S., Klementiev Konstantin E., Goryachev Sergey N., Marcus Moldenhauer, Thomas Friedrich, Los Dmitry A., Paschenko Vladimir Z., Rubin Andrew B.
Журнал: Biophysical Journal
Том: 113
Номер: 2
Год издания: 2017
Издательство: Biophysical Society
Местоположение издательства: United States
Первая страница: 402
Последняя страница: 414
DOI: 10.1016/j.bpj.2017.06.002
Аннотация: Orange Carotenoid Protein (OCP) is known as an effector and regulator of cyanobacterial photoprotection. This 35 kDa water-soluble protein provides specific environment for blue-green light absorbing keto-carotenoids, which excitation causes dramatic but fully reversible rearrangements of the OCP structure, including carotenoid translocation and separation of C- and N-terminal domains upon transition from the basic orange to photoactivated red OCP form. While recent studies greatly improved our understanding of the OCP photocycle and interaction with phycobilisomes and the fluorescence recovery protein, the mechanism of OCP assembly remains unclear. Apparently, this process requires targeted delivery and incorporation of a highly hydrophobic carotenoid molecule into the water-soluble apoprotein of OCP. Recently, we introduced a novel carotenoid carrier protein, COCP, which consists of dimerized C-domain(s) of OCP and can combine with the isolated N-domain to form transient OCP-like species. Here, we demonstrate that in vitro COCP efficiently transfers otherwise tightly bound carotenoid to the full-length OCP apoprotein, resulting in formation of photoactive OCP from completely photoinactive species. We accurately analyze the peculiarities of this process which, to the best of our knowledge, appears unique, previously uncharacterized protein-to-protein carotenoid transfer mechanism. We hypothesize that a similar OCP assembly can occur in vivo, substantiating specific roles of the COCP carotenoid carrier in cyanobacterial photoprotection.
Добавил в систему: Максимов Евгений Георгиевич

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The unique protein-to-protein carotenoid transfer mechanismстатья

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