CYANOBACTERIAL THYLAKOID MEMBRANE-PROTEINS ARE REVERSIBLY PHOSPHORYLATED UNDER PLASTOQUINONE-REDUCING CONDITIONS INVITRO

被引：30

作者：

HARRISON, MA ^{[1
]}

TSINOREMAS, NF ^{[1
]}

ALLEN, JF ^{[1
]}

机构：

[1] UNIV LEEDS,DEPT PURE & APPL BIOL,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND

来源：

FEBS LETTERS | 1991年 / 282卷 / 02期

关键词：

PHOTOSYNTHESIS; PROTEIN PHOSPHORYLATION; STATE TRANSITION; PROTEIN KINASE; PHOSPHATASE; CYANOBACTERIUM;

D O I：

10.1016/0014-5793(91)80499-S

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Reversible, light-dependent protein phosphorylation was observed in isolated thylakoid membranes of the cyanobacterium Synechococcus 6301. A polypeptide of 15 kDa in particular was phosphorylated under plastoquinone-reducing conditions and was not phosphorylated under plastoquinone-oxidising conditions. Phosphorylation and dephosphorylation reactions involving this and several other membrane polypeptides showed sensitivity to inhibitors of protein kinases and phosphatases. Changes in phosphorylation state correlated with changes in low temperature fluorescence emission characteristic of changes in excitation energy distribution between the photosystems. The kDa phosphopolypeptide is likely to be involved directly in light state adaptations in cyanobacteria.

引用

页码：295 / 299

页数：5

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