Characterization of the preferred cation cofactors of chloroplast protein kinases in Arabidopsis thaliana

被引:2
|
作者
Espinoza-Corral, Roberto [1 ,3 ]
Schwenkert, Serena [2 ]
Schneider, Anja [2 ]
机构
[1] Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI USA
[2] Ludwig Maximilians Univ Munchen, Fac Biol, Plant Mol Biol, Planegg, Germany
[3] Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA
来源
FEBS OPEN BIO | 2023年 / 13卷 / 03期
关键词
Arabidopsis; cation homeostasis; chloroplast; protein phosphorylation; STATE TRANSITIONS; PHOSPHORYLATION; IDENTIFICATION; ACCLIMATION; EXTRACTION; MECHANISM; REVEALS;
D O I
10.1002/2211-5463.13563
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chloroplasts sense a variety of stimuli triggering several acclimation responses. One prominent response is the mechanism of state transitions, which enables rapid adaption to changes in illumination. Here, we investigated the link between divalent cations (calcium, magnesium, and manganese) and protein kinase activity in Arabidopsis chloroplasts. Our results show that manganese ions are the strongest activator of kinase activity in chloroplasts followed by magnesium ions, whereas calcium ions are not able to induce kinase activity. Additionally, the phosphorylation of specific protein bands is strongly reduced in chloroplasts of a cmt1 mutant, which is impaired in manganese import into chloroplasts, as compared to the wild-type. These findings provide insights for the future characterization of chloroplast protein kinase activity and potential target proteins.
引用
收藏
页码:511 / 518
页数:8
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