Processing of the D1 polypeptide of the photosystem II reaction centre and photoactivation of a low fluorescence mutant (LF‐1) of Scenedesmus obliquus

FEBS Letters

Packer, J.C.L.¹  Bowyer, J.R.¹  Taylor, M.A.¹ 

[1] Department of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham Hill, Egham TW20 0EX, England

关键词: Photoactivation;    Carboxyl-terminal processing;    D1 polypeptide;    Photosystem II;    (Scenedesmus obliquus);    PS II;    photosystem II;    LF-;    low fluorescence;    C-terminus;    carboxyl terminus of protein;    N-terminus;    amino terminus of protein;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    PBQ;    phenyl-p-benzoquinone;    DCPIP;    2;    6-dichloro-phenolindophenol;   

DOI  :  10.1016/0014-5793(88)80207-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the LF-1 mutant of Scenedesmus obliquus, a failure to remove a C-terminal extension from the D1 protein of photosystem II (PS II) is associated with the absence of a water-splitting manganese complex. Treatment of LF-1 thylakoids and PS II-enriched membranes with a Triton X-100 extract of wild-type thylakoids results in a specific reduction in molecular mass of the LF-1 D1 to the same value as that in wild-type membranes. Water-splitting activity can be photogenerated in these extract-treated LF-1 PS II-enriched membranes, and in PS II membranes from dark-grown wild-type cells, but not in untreated LF-1 membranes. The results indicate that LF-1 cells lack the D1 processing protease, and that the presence of the D1 extension in LF-1 is directly responsible for preventing assembly of the manganese complex.

【 授权许可】

Unknown