A Similar Structure of the Herbicide Binding Site in Photosystem II of Plants and Cyanobacteria is Demonstrated by Site Specific Mutagenesis of the PsbA Gene

Overview

Journal Photosynth Res

Publisher Springer

Date 2014 Jan 15

PMID 24420994

Citations 3

Authors

N Ohad

J Hirschberg

Affiliations

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Abstract

Many herbicides inhibit the photosynthetic electron transfer in photosystem II by binding to the polypeptide D1. A point mutation in the chloroplast gene psbA, which leads to a change of the amino acid residue 264 of D1 from serine to glycine, is responsible for atrazine resistance in higher plants. We have changed serine 264 to glycine in Synechococcus PCC7942 and compared its phenotype to a mutant with a serine to alanine shift in the same position. The results show that glycine at position 264 in D1 gives rise to a similar phenotype in cyanobacteria and in higher plants, indicating a similar structure of the binding site for herbicides and for the quinone QB in the two systems. A possible mode of binding of phenyl-urea herbicides to D1 is predicted from the difference in herbicidal cross-resistance between glycine and alanine substitutions of serine 264.

Citing Articles

Binding affinity of bicarbonate and formate in herbicide-resistant D1 mutants of Synechococcus sp. PCC 7942.

Cao J, Ohad N, Hirschberg J, Xiong J, Govindjee Photosynth Res. 2014; 34(3):397-408.

PMID: 24408835 DOI: 10.1007/BF00029814.

The primary structure of D1 near the QB pocket influences oxygen evolution.

Etienne A, Kirilovsky D Photosynth Res. 2013; 38(3):387-94.

PMID: 24317994 DOI: 10.1007/BF00046765.

Novel psbA1 gene from a naturally occurring atrazine-resistant cyanobacterial isolate.

Sajjaphan K, Shapir N, Judd A, Wackett L, Sadowsky M Appl Environ Microbiol. 2002; 68(3):1358-66.

PMID: 11872488 PMC: 123757. DOI: 10.1128/AEM.68.3.1358-1366.2002.

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