Photoinduced degradation of the D1 protein in isolated thylakoids and various photosystem II particles after donor‐side inactivations Detection of a C‐terminal 16 kDa fragment

FEBS Letters

Barbato, Roberto¹  Friso, Giulia¹  Giacometti, Giorgio Mario¹  Frizzo, Annalisa¹  Rigoni, Fernanda¹ 

[1] Dipartimento di Biologia, Università di Padova, Via Trieste 75, I-35121 Padova, Italy

关键词: Photosynthesis;    Photosystem II;    D1 polypeptide;    Photoinhibition;    Spinacia oleracea;    chl;    chlorophyll;    DBMIB;    2;    5-dibromo-3-methyl-6-isopropyl-p-benzoquinone;    DCPIP;    2;    6-dichlorophenolindophenol;    DPC;    2;    2′-diphenylcarbonic dihydrazide;    HEPES;    N-[2-hydroxyethyl]piperazine-N′-[2-ethanesulfonic acid];    LHC;    light harvesting complex;    PAGE;    polyacrylamide gel electrophoresis;    PS;    photosystem;    P680;    primary donor of photosystem II;    RC;    reaction center complex of photosystem II;    SDS;    sodium dodecyl sulfate;    TRIS;    tris(hydroxymethyl)aminomethane;    Tyrz;    tyrosine 161 on the D1 protein;   

DOI  :  10.1016/0014-5793(92)80604-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Photoinduced degradation of the photosystem II (PSII) reaction center D1 protein was studied in isolated thylakoids and different PSII subparticles. A 16 kDa fragment corresponding to the C-terminus of the protein is detected in thylakoids when they are inactivated at the donor side before illumination. The same D1 fragment is found in different types of PSII preparations at different integration levels characterized by different polypeptide compositions so long as they have an inactivated donor side and an active electron acceptor for the reduced pheophytin. However, when the PSII particle is equal to or smaller than the 43-less PSII core complex, other fragments are observed which are not found in more integrated systems.

【 授权许可】

Unknown