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首页> 外文期刊>Biochimica et biophysica acta. Bioenergetics >Dephosphorylation of photosystem II proteins and phosphorylation of CP29 in barley photosynthetic membranes as a response to water stress.
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Dephosphorylation of photosystem II proteins and phosphorylation of CP29 in barley photosynthetic membranes as a response to water stress.

机译:大麦光合膜中光系统II蛋白的去磷酸化和CP29的磷酸化作为对水分胁迫的响应。

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摘要

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.
机译:大麦类囊体膜中蛋白质去磷酸化的动力学研究表明,光系统II(PSII)蛋白质加速了去磷酸化,同时在水分胁迫下迅速诱导了光收集复合物(LHCII)b4,CP29的磷酸化。复水后,去磷酸化的抑制作用加剧了应力破坏并阻碍了光系统的恢复。内在和外在膜蛋白磷酸酶均催化这种增加的去磷酸化作用。水分胁迫并没有导致类囊体脱壳,并且从颗粒膜向基质暴露的薄片的侧向迁移仅发现于CP29,而未发现其他PSII蛋白。在水分胁迫期间,质体蛋白酶的活化和膜磷酸酶的抑制剂TLP40的释放也得到增强。 CP29的磷酸化可能促进LHCII与PSII复合物的解离,LHCII三聚体的分解及其随后的降解,而PSII蛋白的一般去磷酸化可能参与PSII蛋白的修复周期和应激反应信号转导。

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