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Haworth P, Steinback KE. Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2. Plant Physiol. 1987;83(4):1027-31doi: 10.1104/pp.83.4.1027.
Haworth, P., & Steinback, K. E. (1987). Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2. Plant physiology, 83(4), 1027-31. https://doi.org/10.1104/pp.83.4.1027
Haworth, P, and Steinback, K E. "Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2." Plant physiology vol. 83,4 (1987): 1027-31. doi: https://doi.org/10.1104/pp.83.4.1027
Haworth P, Steinback KE. Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2. Plant Physiol. 1987 Apr;83(4):1027-31. doi: 10.1104/pp.83.4.1027. PMID: 16665318; PMCID: PMC1056495.
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Plant Physiol. 1987 Apr;83(4):1027-31. doi: 10.1104/pp.83.4.1027.

Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2.

Plant physiology

P Haworth, K E Steinback

Affiliations

  1. Zoecon Research Institute, Sandoz Crop Protection Corporation, Palo Alto, California 94304.

PMID: 16665318 PMCID: PMC1056495 DOI: 10.1104/pp.83.4.1027

Abstract

We have used the diuron-resistant Dr2 mutant of Chlamydomonas reinhardtii which is altered in the 32 kilodalton Q(B)-protein at amino acid 219 (valine to isoleucine), to investigate the interactions of herbicides and plastoquinone with the 32 kilodalton Q(B)-protein. The data contained in this report demonstrate that the effects of this mutation are different from those of the more completely characterized mutant which confers extreme resistance to triazines in higher plants. The mutation in C. reinhardtii Dr2 confers only slight resistance to a number of inhibitors of photosynthetic electron transport. Extreme triazine resistance results from an increase in the binding constant of the herbicide with the 32 kilodalton Q(B)-protein, in contrast the diuron binding constant for chloroplasts isolated from wild-type (sensitive) Chlamydomonas and the resistant Dr2 are indistinguishable. We conclude that the altered structure in the 32 kilodalton Q(B)-protein of Dr2 does not directly affect the diuron binding site. This mutation appears to alter the steric properties of the binding protein in such a way that diuron and plastoquinone do not directly compete for binding. This steric perturbation confers mild resistance to other herbicidal inhibitors of photosynthesis and alters the kinetics of Q(A) to Q(B) electron transfer.

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