Evidence for different binding sites on the 33‐kDa protein for DCMU, atrazine and QB

FEBS Letters

Boussac, Alain¹  Etienne, Anne-Lise¹  Astier, Chantal¹ 

[1] Laboratoire de Photosynthèse, CNRS, BP 1, 91190 Gif-sur-Yvette, France

关键词: Cyanobacteria;    Mutant;    Herbicide;    Photosynthesis;    Photosystem II;    DCMU;    3-(3;    4 dichlorophenyl)-1;    1-dimethylurea;    DCPIP;    2;    6-dichlorophenolindophenol;    Wt;    wild type;    PS II;    Photosystem II;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(84)80150-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two DCMU-resistant strains of the cyanobacterium Synechocystis 6714 were used to analyse the binding sites of DCMU, atrazine and Q_B. DCMU^r-II_A was DCMU and atrazine resistant; it presented an impaired electron flow and its 33-kDa protein was weakly attached to the membrane. DCMU^r-II_B, derived from the former, simultaneously regained atrazine sensitivity, normal electron flow and a tight linkage of the 33-kDa protein to the membrane. This mutant shows that loss of DCMU binding does not necessarily affect the binding of either atrazine or Q_B. The role of the 33-kDa protein is discussed.

【 授权许可】

Unknown