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J. Biol. Chem., Vol. 265, Issue 26, 15357-15360, 09, 1990
FE Callahan, ML Ghirardi, SK Sopory, AM Mehta, M Edelman and AK Mattoo
Two forms of the 32 kDa-D1 reaction center protein of photosystem II
(PSII), having slightly different mobilities on denaturing polyacrylamide
gels, have been resolved in Spirodela oligorrhiza, Glycine max L.,
Gossypium hirsutum L., Triticum aestivum L., and Zea mays L. The protein
band with faster mobility is identified as the 32 kDa-D1 protein, and the
less mobile band as a novel form, designated 32*. The two forms are
structurally similar based on immunological and partial proteolytic tests.
32* is associated exclusively with the grana and is present in the PSII
reaction center. Temporally, 32* appears several hours after the
translocation of newly synthesized and processed 32 kDa-D1 protein from the
stroma lamellae to the grana. Formation of the 32* is strictly
light-dependent under physiological light intensities and correlates with a
reciprocal loss of the 32-kDa form. Light induced formation of 32* is
inhibited by 3-(3,4- dichlorophenyl)-1,1-dimethylurea but is not coupled to
linear electron transport.
A novel metabolic form of the 32 kDa-D1 protein in the grana-localized reaction center of photosystem II
Plant Molecular Biology Laboratory, United States Department of Agriculture-ARS, Beltsville Agricultural Research Center (West), Maryland 20705.
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