Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 96:26-31 (1991)
© 1991 American Society of Plant Biologists

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Cellular and Structural Biology

Colocalization of Polyphenol Oxidase and Photosystem II Proteins

Alan R. Lax and Kevin C. Vaughn

U.S. Department of Agriculture, Agricultural Research Service, Southern Regional Research Center, New Orleans, Louisiana, U.S. Department of Agriculture, Agricultural Research Service, Southern Weed Science Laboratory, Stoneville, Mississippi

Polyphenol oxidase (PPO) appears to be ubiquitous in higher plants but, as yet, no function has been ascribed to it. Herein, we report on the localization of PPO based upon biochemical fractionation of chloroplast membranes in Vicia faba (broad bean) into various complexes and immunocytochemical electron microscopic investigations. Sucrose density gradient fractionations of thylakoid membranes after detergent solubilization reveals that PPO protein (by reactivity with anti-PPO antibody) and activity (based upon ability to oxidize dI-dihydroxyphenylalanine) are found only in fractions enriched in photosystem II (PSII). Furthermore, of the PSII particles isolated using three different protocols utilizing several plant species, all had PPO. Immunogold localization of PPO on thin sections reveals exclusive thylakoid labeling with a distribution pattern consistent with other PSII proteins (80% grana, 20% stroma). These data strongly indicate that PPO is at least peripherally associated with the PSII complex.




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M.-H. Cho, S. G. A. Moinuddin, G. L. Helms, S. Hishiyama, D. Eichinger, L. B. Davin, and N. G. Lewis
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[Abstract] [Full Text] [PDF]


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Copyright © 1991 by the American Society of Plant Biologists