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Direct evidence for cooperation of the 17‐ and 23‐kDa proteins in the recovery of oxygen evolution in cholate‐treated thylakoids
Author(s) -
Fukutaka Eitaro,
Imaoka Akiko,
Akabori Kozo,
Toyoshima Yoshinori
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80581-x
Subject(s) - thylakoid , chemistry , tricine , sodium cholate , biochemistry , chromatography , spinach , chloroplast , biophysics , membrane , photosystem ii , oxygen evolution , photosynthesis , biology , electrode , gene , electrochemistry
Repeated extractions of spinach thylakoid membranes with a solution containing 50 mM sodium cholate, 1 M NaCl, 3 mM MgCl 2 , 0.2 M sucrose and 20 mM tricine at pH 8.4 for 15 min perfectly inhibited the O 2 evolution of the thylakoids, concomitant with a complete release of the 17‐ and 23‐kDa proteins and partial release of many other proteins from the thylakoid membranes. Recovery of O 2 evolution in the cholate‐treated thylakoids was achieved up to about 40% of that in the original thylakoids by the simultaneous reinsertion of the 17‐ and 23‐kDa proteins, but not by the reinsertion of one of them only. The recovery of O 2 evolution induced by the reinsertion of the 17‐ and 23‐kDa proteins was enhanced by the further addition of a certain fraction of the crude thylakoid extract up to about 70% of the non‐depleted control, suggesting that in addition to the 17‐ and 23‐kDa proteins, one or more unknown component(s) released partially from the thylakoids upon cholate treatment is (are) also (a) constituent(s) of the O 2 evolving apparatus. The purified 34‐kDa protein did not replace the unknown component.