期刊
PLANT JOURNAL
卷 78, 期 6, 页码 1003-1013出版社
WILEY
DOI: 10.1111/tpj.12525
关键词
chloroplast; protein disulfide isomerase; photoinhibition; photosystem II; D1 turnover; Arabidopsis thaliana
资金
- Israeli Science Foundation
- Minerva Foundation
- Charles W. and Tillie K. Lubin Center for Plant Biotechnology at the Weizmann Institute of Science (Rehovot, Israel)
A chloroplast protein disulfide isomerase (PDI) was previously proposed to regulate translation of the unicellular green alga Chlamydomonas reinhardtii chloroplast psbA mRNA, encoding the D1 protein, in response to light. Here we show that AtPDI6, one of 13 Arabidopsis thalianaPDI genes, also plays a role in the chloroplast. We found that AtPDI6 is targeted and localized to the chloroplast. Interestingly, AtPDI6 knockdown plants displayed higher resistance to photoinhibition than wild-type plants when exposed to a tenfold increase in light intensity. The AtPDI6 knockdown plants also displayed a higher rate of D1 synthesis under a similar light intensity. The increased resistance to photoinhibition may not be rationalized by changes in antenna or non-photochemical quenching. Thus, the increased D1 synthesis rate, which may result in a larger proportion of active D1 under light stress, may led to the decrease in photoinhibition. These results suggest that, although the D1 synthesis rates observed in wild-type plants under high light intensities are elevated, repair can potentially occur faster. The findings implicate AtPDI6 as an attenuator of D1 synthesis, modulating photoinhibition in a light-regulated manner.
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