期刊
MOLECULAR PLANT
卷 10, 期 1, 页码 115-130出版社
CELL PRESS
DOI: 10.1016/j.molp.2016.10.001
关键词
Chlamydomonas reinhardtii; chlorophyll b-less mutant; antenna protein; CAO gene
资金
- CNRS
- Universite Pierre & Marie Curie Paris
- Agence Nationale de la Recherche [ANR-12-BSV8-0011]
- Initiative d'Excellence program from the French State (Grant 'DYNAMO') [ANR-11-LABX-0011-01]
- Japan Science and Technology Agency (JST), CREST
- JSPS KAKENHI [15K14551, 16H06554]
- DST-JSPS India-Japan Cooperative Science Program [13039221-000325]
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV8-0011] Funding Source: Agence Nationale de la Recherche (ANR)
- Grants-in-Aid for Scientific Research [16H06554, 15K14551] Funding Source: KAKEN
The green alga Chlamydomonas reinhardtii contains several light-harvesting chlorophyll a/b complexes (LHC): four major LHCIIs, two minor LHCIIs, and nine LHCIs. We characterized three chlorophyll b-less mutants to assess the effect of chlorophyll b deficiency on the function, assembly, and stability of these chlorophyll a/b binding proteins. We identified point mutations in two mutants that inactivate the CAO gene responsible for chlorophyll a to chlorophyll b conversion. All LHCIIs accumulated to wild-type levels in a CAO mutant but their light-harvesting function for photosystem II was impaired. In contrast, most LHCIs accumulated to wild-type levels in the mutant and their light-harvesting capability for photosystem I remained unaltered. Unexpectedly, LHCI accumulation and the photosystem I functional antenna size increased in the mutant compared with in the wild type when grown in dim light. When the CAO mutation was placed in a yellow-in-the-dark background (yid-BF3), in which chlorophyll a synthesis remains limited in dim light, accumulation of the major LHCIIs and of most LHCIs was markedly reduced, indicating that sustained synthesis of chlorophyll a is required to preserve the proteolytic resistance of antenna proteins. Indeed, after crossing yid-BF3 with a mutant defective for the thylakoid FtsH protease activity, yid-BF3-ftsh1 restored wild-type levels of LHCI, which defines LHCI as a new substrate for the FtsH protease.
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