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大麦光合膜中光系统II蛋白的去磷酸化和CP29的磷酸化对水分胁迫的响应

Dephosphorylation of photosystem II proteins and phosphorylation of CP29 in barley photosynthetic membranes as a response to water stress.

作者信息

Liu Wen-Juan, Chen Yang-Er, Tian Wen-Juan, Du Jun-Bo, Zhang Zhong-Wei, Xu Fei, Zhang Fan, Yuan Shu, Lin Hong-Hui

机构信息

Ministry of Education Key Laboratory for Bio-Resource and Eco-Environment, College of Life Science, Sichuan University, Chengdu, China.

出版信息

Biochim Biophys Acta. 2009 Oct;1787(10):1238-45. doi: 10.1016/j.bbabio.2009.04.012. Epub 2009 May 3.

Abstract

Kinetic studies of protein dephosphorylation in barley thylakoid membranes revealed accelerated dephosphorylation of photosystem II (PSII) proteins, and meanwhile rapidly induced phosphorylation of a light-harvesting complex (LHCII) b4, CP29 under water stress. Inhibition of dephosphorylation aggravates stress damages and hampers photosystem recovery after rewatering. This increased dephosphorylation is catalyzed by both intrinsic and extrinsic membrane protein phosphatase. Water stress did not cause any thylakoid destacking, and the lateral migration from granum membranes to stroma-exposed lamellae was only found to CP29, but not other PSII proteins. Activation of plastid proteases and release of TLP40, an inhibitor of the membrane phosphatases, were also enhanced during water stress. Phosphorylation of CP29 may facilitate disassociation of LHCII from PSII complex, disassembly of the LHCII trimer and its subsequent degradation, while general dephosphorylation of PSII proteins may be involved in repair cycle of PSII proteins and stress-response-signaling.

摘要

大麦类囊体膜中蛋白质去磷酸化的动力学研究表明,在水分胁迫下,光系统II(PSII)蛋白的去磷酸化加速,同时光捕获复合体(LHCII)b4、CP29迅速诱导磷酸化。去磷酸化的抑制会加重胁迫损伤,并阻碍复水后光系统的恢复。这种增加的去磷酸化由内在和外在膜蛋白磷酸酶催化。水分胁迫未导致任何类囊体垛叠解体,仅发现CP29从基粒膜侧向迁移到基质暴露的片层,而其他PSII蛋白未出现这种情况。在水分胁迫期间,质体蛋白酶的激活以及膜磷酸酶抑制剂TLP40的释放也增强。CP29的磷酸化可能促进LHCII从PSII复合体解离、LHCII三聚体的解体及其随后的降解,而PSII蛋白的普遍去磷酸化可能参与PSII蛋白的修复循环和应激反应信号传导。

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