Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 79:1118-1124 (1985)
© 1985 American Society of Plant Biologists

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Topography of the Protein Complexes of the Chloroplast Thylakoid Membrane 1

Studies of Photosystem II using Pronase Digestion and Chemical Labeling

Eric Lam2 and Richard Malkin

Division of Molecular Plant Biology, University of California, Berkeley, California 94720

The accessibility of various Photosystem II (PSII)-associated polypeptides to the protease pronase and the chemical modifier trinitrobenzene-sulfonic acid (TNBS) has been investigated. Three polypeptides with apparent molecular weight of 32, 21, and 16 kilodaltons, known to be associated with O2 evolution, are all resistant to pronase digestion and TNBS labeling in intact thylakoids. All the polypeptides in the isolated PSII preparation were labeled with TNBS while a different pattern of labeling was observed when the PSII complex was isolated from TNBS-modified thylakoids. Attempts to prepare PSII particles from pronase-treated thylakoids using the Triton X-100 solubilization method were unsuccessful. Pronase-treated thylakoids were probed with antisera against the chlorophyll proteins of PSII using immunoblotting techniques. This allowed for a positive identification of proteolytic fragments from the respective proteins. The results are discussed in relation to the transmembrane organization of PSII in spinach thylakoids.

2 Present address: Laboratory of Plant Molecular Biology, Rockefeller University, New York, NY 10021.

1 Supported in part by a grant from the National Science Foundation.






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Copyright © 1985 by the American Society of Plant Biologists