| Literature DB >> 10773168 |
Abstract
The study of turnover of two distinct forms of the photosystem II (PSII) D1 protein in cells of the cyanobacterium Synechococcus PCC 7942 showed that the 'high-light' form D1:2 is degraded significantly faster at 500 microE m(-2) s(-1) as compared with 50 microE m(-2) s(-1) while the degradation rates of the 'low-light' form D1:1 under low and high irradiance are not substantially different. Consequently, the D1:1 turnover does not match photoinactivation of PSII under increased irradiance and therefore the cells containing this D1 form exhibit a decrease in the PSII activity. Monitoring of the content of each D1 form during a recovery from growth-temperature photoinhibition showed a good correlation between the synthesis of D1:2 and restoration of the PSII activity. In contrast, when photoinhibitory treatment was conducted at low temperature, a fast recovery was not accompanied by the D1:2 accumulation. The data suggest that photoinactivation at growth temperature results in a modification of PSII that inhibits insertion of D1:1 and, therefore, for restoration of the photochemical activity in the photoinactivated PSII complexes the D1:2 synthesis is needed. This may represent the primary reason for the requirement of psbAII/psbAIII expression under increased irradiance.Entities:
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Year: 2000 PMID: 10773168 DOI: 10.1016/s0005-2728(00)00105-5
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002