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Abstract

A) We have carried out a molecular and genetic analysis of the chloroplast ATPase in Chlamdydomonas Reinhardtii. Recombination and complementation studies on 16 independently isolated chloroplast mutations affecting this complex demonstrated that they represent alleles in five distinct chloroplast genes. B) We report the isolation and characterization of a uniparental mutant of Chlamydomonas Reinhardtii that is resistant to DCMU and atrazine. Such herbicides inhibit photosynthesis by preventing transfer of electrons in Photosystem II from the primary stable electron acceptor Q to the secondary stable electron acceptor complex, B, which is thought to contain a protein of 32 kilodaltons (KDal) and a bound quinone. We have isolated IpsbAR, the chloroplast gene for the 32 kDal protein, from both wild-type and herbicide resistant algae and sequenced the coding regions of the gene which are contained in five exons. This mutation results in a predicted amino acid change of serine in the wild-type protein to alanine in the mutant. We suggest that this alteration in the 32 kDal protein is the molecular basis for herbicide resistance in the C. Reinhardtii mutant.

Additional information

Authors: BEMMOUN P, INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE);GIRARD J, INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE);MASSON A, INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE);DELEPELAIRE P, INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE);WOLLMAN F A INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE), INSTITUT DE BIOLOGIE PHYSICO-CHIMIQUE, PARIS (FRANCE)
Bibliographic Reference: EUR 9322 EN (1984) MF, 58 P., BFR 120 BLOW-UP COPY OF BFR 290, EUROFFICE, LUXEMBOURG, POB 1003
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