
Turnover of thylakoid photosystem II proteins during photoinhibition of Chlamydomonas reinhardtii
Author(s) -
SCHUSTER Gadi,
TIMBERG Rina,
OHAD Itzhak
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14388.x
Subject(s) - photoinhibition , chlamydomonas reinhardtii , photosystem ii , thylakoid , photosystem i , biology , photosynthesis , biophysics , photosynthetic reaction centre , chloroplast , biochemistry , chemistry , gene , mutant
The turnover of photosystem‐II proteins during photoinhibition was analyzed in the green alga Chlamydomonas reinhardtii . Changes in the amount of photosystem II core complex polypeptides D1, D2, 44 kDa and 51 kDa, the antennae‐CP‐29 and light‐harvesting‐complex‐II polypeptides and the water‐oxidizing complex polypeptides of 30 kDa, 23 kDa and 16 kDa were monitored by a variety of techniques. Only the D1 and D2 polypeptides were found to turnover during photoinhibition when cells were exposed to ten fold photosynthesis‐saturating light (2500 W m 2 for 90 min) at 25°C. While 80% of photosystem‐II activity was lost, a reduction of only 20% was observed in the total amount of D1 and D2 proteins. However, inhibition of chloroplast translation by chloramphenicol during photoinhibition resulted in the loss of about 60% of the D1 and 40% of the D2 proteins, as demonstrated by Western blotting and dot blotting of isolated thylakoids, quantitative analysis of immunogold‐labeled whole‐cell thin sections, and chase of radioactively prelabelled proteins during photoinhibition. We propose that the light‐dependent turnover of the D1 protein is a protective mechanism against photoinhibition as far as the removal and replacement of D1 is compatible with the photoinactivation incurred by photosystem II. At light intensities at which the rate of D1 removal becomes limiting, loss of photosystem‐II activity exceeds the turnover of D1 and the stability of the D2 protein is impaired as well.