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Evidence for different binding sites on the 33‐kDa protein for DCMU, atrazine and Q B
Author(s) -
Astier Chantal,
Boussac Alain,
Etienne Anne-Lise
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80150-7
Subject(s) - dcmu , atrazine , biology , binding site , biophysics , biochemistry , photosystem ii , photosynthesis , ecology , pesticide
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.