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Psb28 protein is indispensable for stable accumulation of PSII core complexes in Arabidopsis

文献类型： 外文期刊

作者： Zhao, Yuwei 1 ; Deng, Linbin 1 ; Last, Robert L. 4 ; Hua, Wei 1 ; Liu, Jun 1 ;

作者机构： 1.Chinese Acad Agr Sci, Key Lab Biol & Genet Improvement Oil Crops, Minist Agr & Rural Affairs, Oil Crops Res Inst, Wuhan 430062, Peoples R China

2.Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Wuhan 430070, Peoples R China

3.Chinese Acad Agr Sci, Grad Sch, Beijing 100081, Peoples R China

4.Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA

5.Michigan State Univ, Dept Plant Biol, E Lansing, MI 48824 USA

关键词： photosynthesis; photosystem II; photosynthetic efficiency; fluctuating light; photoinhibition; photoprotection; Arabidopsis thaliana

期刊名称：PLANT JOURNAL （ 影响因子：7.2； 五年影响因子：7.9 ）

ISSN： 0960-7412

年卷期： 2024 年

页码：

收录情况： SCI

摘要： Enhancing the efficiency of photosynthesis represents a promising strategy to improve crop yields, with keeping the steady state of PSII being key to determining the photosynthetic performance. However, the mechanisms whereby the stability of PSII is maintained in oxygenic organisms remain to be explored. Here, we report that the Psb28 protein functions in regulating the homeostasis of PSII under different light conditions in Arabidopsis thaliana. The psb28 mutant is much smaller than the wild-type plants under normal growth light, which is due to its significantly reduced PSII activity. Similar defects were seen under low light and became more pronounced under photoinhibitory light. Notably, the amounts of PSII core complexes and core subunits are specifically decreased in psb28, whereas the abundance of other representative components of photosynthetic complexes remains largely unaltered. Although the PSII activity of psb28 was severely reduced when subjected to high light, its recovery from photoinactivation was not affected. By contrast, the degradation of PSII core protein subunits is dramatically accelerated in the presence of lincomycin. These results indicate that psb28 is defective in the photoprotection of PSII, which is consistent with the observation that the overall NPQ is much lower in psb28 compared to the wild type. Moreover, the Psb28 protein is associated with PSII core complexes and interacts mainly with the CP47 subunit of PSII core. Taken together, these findings reveal an important role for Psb28 in the protection and stabilization of PSII core in response to changes in light environments.

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