The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP

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• 作者：Nikolai N. Sluchanko^a ; ^{nikolai.sluchanko@mail.ru} ; Konstantin E. Klementiev^b ; Evgeny A. Shirshin^c ; Georgy V. Tsoraev^b ; Thomas Friedrich^d ; Eugene G. Maksimov^b
• 关键词：PBs ; phycobilisomes ; GA ; glutaraldehyde ; OCPO ; Orange Carotenoid Protein &ndash ; orange form ; OCPR ; Orange Carotenoid Protein &ndash ; red form ; OCPW288A ; the purple mutant of the Synechocystis OCP ; FRP ; Fluorescence Recovery Protein ; ECN ; echinenone ; EDTA ; ethylenediaminetetraacetate ; CTD ; C-terminal domain ; NTD ; N-terminal domain ; SEC ; size-exclusion chromatography ; RT ; retention time
• 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1858
• 期：1
• 页码：1-11
• 全文大小：1663 K
• 卷排序：1858

文摘

OCPW288A is capable of PBs fluorescence quenching. PBs quenching mechanisms by OCPR and OCPW288A are equivalent. Like OCPR, OCPW288A binds to FRP at a 1:1 stoichiometry. FRP binding requires its monomerization; causes compaction and “oranging” of OCPW288A. FRP seems to function like an adaptor or scaffold protein relative to OCP.