磷酸化
光合作用
叶绿体
类囊体
生物
拟南芥
激酶
细胞生物学
电子传输链
突变体
蛋白质磷酸化
蛋白激酶A
生物物理学
生物化学
基因
作者
Sonja Reiland,Giovanni Finazzi,Anne Endler,Adrian Willig,Katja Baerenfaller,Jonas Grossmann,Bertran Gerrits,Dorothea Rutishauser,Wilhelm Gruissem,Jean‐David Rochaix,Sacha Baginsky
标识
DOI:10.1073/pnas.1104734108
摘要
Important aspects of photosynthetic electron transport efficiency in chloroplasts are controlled by protein phosphorylation. Two thylakoid-associated kinases, STN7 and STN8, have distinct roles in short- and long-term photosynthetic acclimation to changes in light quality and quantity. Although some substrates of STN7 and STN8 are known, the complexity of this regulatory kinase system implies that currently unknown substrates connect photosynthetic performance with the regulation of metabolic and regulatory functions. We performed an unbiased phosphoproteome-wide screen with Arabidopsis WT and stn8 mutant plants to identify unique STN8 targets. The phosphorylation status of STN7 was not affected in stn8 , indicating that kinases other than STN8 phosphorylate STN7 under standard growth conditions. Among several putative STN8 substrates, PGRL1-A is of particular importance because of its possible role in the modulation of cyclic electron transfer. The STN8 phosphorylation site on PGRL1-A is absent in both monocotyledonous plants and algae. In dicots, spectroscopic measurements with Arabidopsis WT, stn7 , stn8, and stn7 / stn8 double-mutant plants indicate a STN8-mediated slowing down of the transition from cyclic to linear electron flow at the onset of illumination. This finding suggests a possible link between protein phosphorylation by STN8 and fine-tuning of cyclic electron flow during this critical step of photosynthesis, when the carbon assimilation is not commensurate to the electron flow capacity of the chloroplast.
科研通智能强力驱动
Strongly Powered by AbleSci AI