Two sites of primary degradation of the D1‐protein induced by acceptor or donor side photo‐inhibition in photosystem II core complexes

FEBS Letters

De Las Rivas, Javier¹  Andersson, Bertil¹  Barber, James¹ 

[1] AFRC Photosynthesis Research Group, Biochemistry Department, Wolfson Laboratories, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK

关键词: Photo-inhibition;    Photosystem II;    D1-protein;    DBMIB;    2;    5-dibromo-3-methyl-6-isopropyl-p-benzo-quinone;    LHCII;    light harvesting complex II;    PAGE;    polyacrylamide gel electrophoresis;    PSII;    photosystem II;    SDS;    sodium dodecyl sulphate;   

DOI  :  10.1016/0014-5793(92)80250-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Depending on experimental conditions we have found that photo-inhibitory treatment of photosystem II (PSII) core complexes, isolated from wheat, can generate two fragments of about 23–24 kDa that contain either the C-terminal or N-terminal regions of the D1-protein. A 24 kDa C-terminal fragment appears when the water splitting reaction is not functional and an electron acceptor is present. This ‘donor’-side inhibition also generates an N-terminal fragment of about 10 kDa and is suggested to be due to the cleavage of a peptide bond in the region connecting transmembrane segments I and II of the D1-protein. In contrast, an N-terminal 23 kDa D1-protein fragment is detected when the water splitting reactions of the isolated complex are active, and occurs in the absence of an added electron acceptor. This ‘acceptor’-side photo-inhibition also generates a C-terminal fragment of about 10 kDa.

【 授权许可】

Unknown