Detection of a 10 kDa breakdown product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism.
Photoinhibition of intact leaves of wheat generates a 10 kDa breakdown product which is clearly observed both at 4 degrees C and 25 degrees C. Selective immunoblotting has shown that the 10 kDa fragment contains the C-terminus of the D1-protein and, under the conditions employed, supports an acceptor side mechanism for photoinhibition in vivo. Although a corresponding 23 kDa N-terminal D1-fragment was not detected our results are consistent with the argument that the primary cleavage site is in the loop joining putative transmembrane segments IV and V.
Cánovas
P M
PM
Wolfson Laboratories, Biochemistry Department, Imperial College of Science, Technology and Medicine, London, UK.
Barber
J
J
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D008027:Light; D010446:Peptide Fragments / Q000378:metabolism; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D014908:Triticum
D001426:Bacterial Proteins; D010446:Peptide Fragments; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins