TY - JOUR
T1 - Characterization of chloroplast thylakoid polypeptides in the 32-kDa region
T2 - Polypeptide extraction and protein phosphorylation affect binding of photosystem II-directed herbicides
AU - Vermaas, Wim F.J.
AU - Steinback, Katherine E.
AU - Arntzen, Charles J.
N1 - Funding Information:
i Journal Article 11037 from the Michigan cultural Experiment Station. a Supported, in part, by DOE Contract DE-ACOZ-76ERO-1338 to MSU and a grant from Advanced Genetic Sciences to K. E. Steinback. a Current address: Vakgroep Plantenfysiologisch Onderzoek, Landbouwhogeschool, Gen. Foulkesweg 6703 BW Wageningen, The Netherlands. 4 To whom correspondence should be addressed: Advanced Genetic Sciences, Inc., 6701 San Pablo Ave., Oakland, Calif. 94608. ’ Abbreviations used: atrazine, amino-6-(isopropylamino)-s-triazine; 4-azido-2-isopropylamino-6-ethylamino-s-triazine; B, the secondary electron accepting plastoquinone in Photosystem II; CBB, Coomassie brilliant blue; chl, chlorophyll; dinoseb, 2-set-butyl-4,6-dinitrophenol; diuron, 3-(3,4-dichlorophenyl)-l,l-dimethylurea; HBP-32, herbicide binding polypeptide of 32 kDa; ioxynil, 4-hydroxy-3,5-diiodobenzonitrile; LRP-32, lysine-rich polypeptide of 32 kDa; PS II, Photosystem II; Q, the primary electron accepting plastoquinone in Photo-
PY - 1984/5/15
Y1 - 1984/5/15
N2 - 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.
AB - 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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U2 - 10.1016/0003-9861(84)90382-5
DO - 10.1016/0003-9861(84)90382-5
M3 - Article
C2 - 6372695
AN - SCOPUS:0021763505
SN - 0003-9861
VL - 231
SP - 226
EP - 232
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -