Light‐dependent N‐terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii
Light‐dependent N‐terminal phosphorylation of LHCSR3 and LHCB4 are interlinked in Chlamydomonas reinhardtii
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DOI：
10.1111/tpj.14368
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发表时间：
2019-05
期刊：
影响因子：
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通讯作者：
M. Scholz;Philipp Gäbelein;Huidan Xue;Laura Mosebach;S. V. Bergner;M. Hippler
中科院分区：
文献类型：
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作者：
M. Scholz;Philipp Gäbelein;Huidan Xue;Laura Mosebach;S. V. Bergner;M. Hippler
本研究利用定量蛋白质组学和基因工程技术对莱茵衣藻LHCSR 3的磷酸化动力学进行了研究。在强光下诱导LHCSR 3蛋白表达和磷酸化。我们的数据揭示了协同和动态的N-末端LHCSR 3磷酸化。磷酸化和非磷酸化LHCSR 3与PSII-LHCII超复合物相关。LHCB 4的磷酸化状态与LHCSR 3 N末端多个位点的磷酸化密切相关，表明LHCSR 3磷酸化可能作为调节LHCB 4磷酸化的分子开关，这反过来对PSII-LHCII分解很重要。值得注意的是，LHCSR 3磷酸化在长时间的强光下减少，这与CEF的发生一致。显着改变的蛋白质的层次聚类显示LHCSR 3，CRX和FNR的表达谱相似。这一发现表明LHCSR 3蛋白丰度与磷酸化、光合电子流和氧化应激反应之间存在功能联系。
Summary Phosphorylation dynamics of LHCSR3 were investigated in Chlamydomonas reinhardtii by quantitative proteomics and genetic engineering. LHCSR3 protein expression and phosphorylation were induced in high light. Our data revealed synergistic and dynamic N‐terminal LHCSR3 phosphorylation. Phosphorylated and nonphosphorylated LHCSR3 associated with PSII‐LHCII supercomplexes. The phosphorylation status of LHCB4 was closely linked to the phosphorylation of multiple sites at the N‐terminus of LHCSR3, indicating that LHCSR3 phosphorylation may operate as a molecular switch modulating LHCB4 phosphorylation, which in turn is important for PSII‐LHCII disassembly. Notably, LHCSR3 phosphorylation diminished under prolonged high light, which coincided with onset of CEF. Hierarchical clustering of significantly altered proteins revealed similar expression profiles of LHCSR3, CRX, and FNR. This finding indicated the existence of a functional link between LHCSR3 protein abundance and phosphorylation, photosynthetic electron flow, and the oxidative stress response.