Characterisation of the D1 protein in a photosystem II mutant (LF‐1) of Scenedesmus obliquus blocked on the oxidising side Evidence supporting non‐processing of D1 as the cause of the lesion

FEBS Letters

Bowyer, J.R.¹  Taylor, M.A.¹  Todd, C.M.¹  Nixon, P.J.²  Barber, J.² 

[1] Department of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham Hill, Egham TW20 0EX, England;AFRC Photosynthesis Research Group, Department of Pure and Applied Biology, Imperial College of Science and Technology, London SW7 2BB, England

关键词: Carboxyl-terminal processing;    D1 polypeptide;    Photosystem II;    psbA gene product;    (Scenedesmus obliquus);    PS II;    photosystem II;    LF-;    low fluorescence;    C-terminus;    carboxyl-terminus of protein;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    azidoatrazine;    2-azido-4-ethylamino-6-isopropylamino-s-triazine;   

DOI  :  10.1016/0014-5793(88)81243-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The D1 polypeptide of the photosystem II reaction centre in a mutant (LF-1) of Scenedesmus obliquus lacking a water-splitting manganese complex is approx. 1.5 kDa larger than that in the wild type but the D2 protein is the same size. The peptide profiles of D1 on partial digestion with papain or endoproteinase Lys-C indicate that the extra segment in the LF-1 protein is located at or near the carboxyl-terminus. The D1 proteins produced by in vitro translation of mRNA from wild type and LF-1 cells have an identical molecular mass to D1 from LF-1 thylakoids whereas D1 from wild-type thylakoids is 1.5 kDa smaller due to C-terminal processing. These results support the hypothesis that in the LF-1 mutant, the D1 protein is incorporated into the PS II reaction centre, but the C-terminal extension is not removed.

【 授权许可】

Unknown