4.7 Article

Quantitative proteomics reveals redox-based functional regulation of photosynthesis under fluctuating light in plants

期刊

JOURNAL OF INTEGRATIVE PLANT BIOLOGY
卷 64, 期 11, 页码 2168-2186

出版社

WILEY
DOI: 10.1111/jipb.13348

关键词

fluctuating light; photosystem I; photosynthesis; redox regulation; thioredoxin

资金

  1. National Natural Science Foundation of China [31970261]
  2. Talent Support Project of Guangdong [2019TQ05N182]

向作者/读者索取更多资源

This study investigates the effects of fluctuating light conditions on the redox regulation of photosynthesis in Arabidopsis thaliana. The research shows that photosystem I (PSI) proteins are key targets of redox regulation and that exposure to fluctuating light results in decreased PSI abundance, stability, and activity. Additionally, the study uncovers the role of the PSI assembly factor PSA3 and thioredoxin m (Trx m) proteins in the redox switching of PSI and the overall functioning of photosynthesis. These findings provide insights into how plants acclimate to changing light conditions.
Photosynthesis involves a series of redox reactions and is the major source of reactive oxygen species in plant cells. Fluctuating light (FL) levels, which occur commonly in natural environments, affect photosynthesis; however, little is known about the specific effects of FL on the redox regulation of photosynthesis. Here, we performed global quantitative mapping of the Arabidopsis thaliana cysteine thiol redox proteome under constant light and FL conditions. We identified 8857 redox-switched thiols in 4350 proteins, and 1501 proteins that are differentially modified depending on light conditions. Notably, proteins related to photosynthesis, especially photosystem I (PSI), are operational thiol-switching hotspots. Exposure of wild-type A. thaliana to FL resulted in decreased PSI abundance, stability, and activity. Interestingly, in response to PSI photodamage, more of the PSI assembly factor PSA3 dynamically switches to the reduced state. Furthermore, the Cys199 and Cys200 sites in PSA3 are necessary for its full function. Moreover, thioredoxin m (Trx m) proteins play roles in redox switching of PSA3, and are required for PSI activity and photosynthesis. This study thus reveals a mechanism for redox-based regulation of PSI under FL, and provides insight into the dynamic acclimation of photosynthesis in a changing environment.

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