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Plant and Cell Physiology, 1998, Vol. 39, No. 6 620-626
© 1998

The Herbicide-Resistant Species of the Cyanobacterial Dl Protein Obtained by Thorough and Random in vitro Mutagenesis

Yoshihiro Narusaka1,2,4, Mari Narusaka1, Hirokazu Kobayashi1,3 and Kimiyuki Satoh2

1 Division of Biological Regulation and Photobiology, National Institute for Basic Biology Okazaki, 444 Japan
2 Department of Biology, Okayama University Okayama, 700 Japan
3 Graduate School of Nutritional and Environmental Sciences, University of Shizuoka Shizuoka, 422 Japan

4 Corresponding author. Present address: Laboratory of Fungicide Chemistry, National Institute of Agro-Environmental Sciences, 3-1-1, Kannondai, Tsukuba, Ibaraki, 305 Japan.

Random mutations were introduced into the DNA fragment of the psbA2 gene of Synechocystis sp. PCC 6803, which encodes the carboxyl-terminal 178 amino acid region of the Dl protein of the PSII reaction center, by in vitro random mutagenesis to obtain Dl species resistant to herbicides and to understand the protein-herbicide interactions. The mutants were screened on the criterion of resistance to either 1 µM DCMU or 10 µM atrazine. In these mutants, amino acid substitutions were distributed throughout the entire area of the targeted region in the Dl protein. However, in every mutant, except for one case, the substitution was present in the region described as the "herbicide-binding niche", i.e., between Phe211 and Leu275, although some amino acid substitutions which were not previously described were found at residues known to be involved with herbicide affinity. Thus, the result of random mutagenesis basically supports the validity of the proposed structural model for the Dl protein, as well as of the herbicide-binding niche. Preliminary characterization of the herbicide-resistant mutants obtained in this study has also been conducted.

(Received December 8, 1997; )
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