Characterization of chloroplast thylakoid polypeptides in the 32-kDa region: polypeptide extraction and protein phosphorylation affect binding of photosystem II-directed herbicides |
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Authors: | W F Vermaas K E Steinback C J Arntzen |
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Affiliation: | MSU/DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824 U.S.A. |
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Abstract: | In order to distinguish between two photosystem II proteins with apparent molecular weights of about 32 kDa, mild extraction procedures were used to remove several thylakoid membrane components. A 32-kDa protein that stained intensely with Coomassie brilliant blue could be extracted from the thylakoid membranes without removing the 32-kDa herbicide receptor protein, which stained poorly with Coomassie brilliant blue. The nonextracted protein was readily detectable after in vivo polypeptide labeling with [35S]methionine or after in vitro covalent tagging with [14C]azidoatrazine. The procedures used to extract the intensely stained, 32-kDa polypeptide resulted in changes in herbicide-binding characteristics, presumably due to conformational changes in the herbicide-binding environment. Alterations of membrane surface charge by protein phosphorylation also influenced herbicide binding. |
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Keywords: | To whom correspondence should be addressed: Advanced Genetic Sciences Inc. 6701 San Pablo Ave. Oakland Calif. 94608. |
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