Herbicide Resistance and Supersensitivity in Ala250 or Ala251 Mutants of the D1 Protein in Chlamydomonas reinhardtii

Abstract Various site-directed mutants at position Ala 250 or Ala 251 within the herbicide-binding niche of the D1 subunit of photosystem II were generated by transforming a Chlamydomonas reinhardtii strain specifically engineered to lack a psb A gene fragment coding for the binding region. The following mutants were obtained: Asp 250 , Phe 250 , His 250 , Ile 250 , Asn 250 , Arg 250 , Tyr 250 , Cys 251 , Gly 251 , and the double mutant Ser 250 /Ile 255 . A variety of herbicides and inhibitors, such as s -triazines, phenolic herbicides, p -benzo- and naphthoquinones, acridones, a NH-thiazol, and phenmedipham, were assayed for their inhibitory activity in these mutants. In addition, in the Ser 250 /Ile 255 mutant 32 different triazinones were tested for biological activity. In all mutants, either resistance and/or supersensitivity against the herbicides and inhibitors was observed. The resistance and/or supersensitivity against inhibitors in the Ala 250 mutants demonstrated for the first time the involvement of this amino acid in herbicide binding.

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