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PLANT PHYSIOLOGY , Vol 111, Issue 4 1183-1190, Copyright © 1996 by American Society of Plant Biologists
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WHOLE PLANT, ENVIRONMENTAL, AND STRESS PHYSIOLOGY |
Degradation Pattern of Photosystem II Reaction Center Protein D1 in Intact Leaves (The Major Photoinhibition-Induced Cleavage Site in D1 Polypeptide Is Located Amino Terminally of the DE Loop)
R. Kettunen, E. Tyystjarvi and E. M. Aro
Department of Biology, University of Turku, FIN-20014 Turku, Finland
Photoinhibition-induced degradation of the D1 protein of the photosystem II
reaction center was studied in intact pumpkin (Cucurbita pepo L.) leaves.
Photoinhibition was observed to cause the cleavage of the D1 protein at two
distinct sites. The main cleavage generated an 18-kD N-terminal and a 20-kD
C-terminal degradation fragment of the D1 protein. This cleavage site was
mapped to be located clearly N terminally of the DE loop. The other,
less-frequent cleavage occurred at the DE loop and produced the
well-documented 23-kD, N-terminal D1 degradation product. Furthermore, the
23-kD, N-terminal D1 fragment appears to be phosphorylated and can be
detected only under severe photoinhibition in vivo. Comparison of the D1
degradation pattern after in vivo photoinhibition to that after in vitro
acceptor-side and donor-side photoinhibition, performed with isolated
photosystem II core particles, gives indirect evidence in support of
donor-side photoinhibition in intact leaves.
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