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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

De Las Rivas J,Andersson B,Barber J

doi

10.1016/0014-5793(92)80250-k

keywords:

subject

Has Abstract

pub_date

1992-04-27 00:00:00

pages

246-52

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80250-K

journal_volume

301

pub_type

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