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D1 protein degradation during photoinhibition of intact leaves a modification of the D1 protein precedes degradation
Author(s) -
Kettunen Reetta,
Tyystjärvi Esa,
Aro Eva-Mari
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81247-6
Subject(s) - photoinhibition , thylakoid , photosystem ii , degradation (telecommunications) , chemistry , protein degradation , biophysics , chloramphenicol , photosynthesis , biochemistry , chloroplast , biology , gene , telecommunications , computer science , antibiotics
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.