D1 protein degradation during photoinhibition of intact leaves. A modification of the D1 protein precedes degradation.
Illumination of intact pumpkin leaves with high light led to severe photoinhibition of photosystem II with no net degradation of the D1 protein. Instead, however, a modified form of D1 protein with slightly slower electrophoretic mobility was induced with corresponding loss in the original form of the D1 protein. When the leaves were illuminated in the presence of chloramphenicol the modified form was degraded, which led to a decrease in the total amount of the D1 protein. Subfractionation of the thylakoid membranes further supported the conclusion that the novel form of the D1 protein was not a precursor but a high-light modified form that was subsequently degraded.
Department of Biology, University of Turku, Finland.
R
R
Kettunen
E
E
Tyystjärvi
E M
EM
Aro
D015153:Blotting, Western; D002736:Chloroplasts / Q000378:metabolism; D008027:Light; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000276:immunology / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D010944:Plants
D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex