Molecular Plant Biology, Department of Biochemistry, University of Turku, Finland.
Institute of Plant Physiology, Laboratory of Intracellular Regulation, Russian Academy of Sciences, Moscow, Russia.
FEBS Lett. 2018 Feb;592(3):411-421. doi: 10.1002/1873-3468.12970. Epub 2018 Feb 1.
In Synechocystis 6803, the ferredoxin 5 (Fd5) phosphoprotein and the S/T protein kinase SpkG are encoded by the slr0148 and slr0152 genes, respectively, which belong to the slr0144-slr0152 cluster. Using a targeted proteomic approach, we showed that SpkG is responsible for the phosphorylation of Fd5 on residues T18 and T72. Sequence alignments and Fd5 structure modelling suggest that these phosphorylation events modulate protein-protein interaction. Furthermore, Fd5 phosphorylation is affected by the Slr0151 protein encoded by the gene preceding spkG in the gene cluster. We propose that Slr0151 functions as an auxiliary protein in the regulation of the ratio between phosphorylated and nonphosphorylated forms of Fd5.
在集胞藻 6803 中，铁氧还蛋白 5（Fd5）磷酸化蛋白和 S/T 蛋白激酶 SpkG 分别由 slr0148 和 slr0152 基因编码，它们属于 slr0144-slr0152 簇。使用靶向蛋白质组学方法，我们表明 SpkG 负责 Fd5 残基 T18 和 T72 的磷酸化。序列比对和 Fd5 结构建模表明，这些磷酸化事件调节蛋白-蛋白相互作用。此外，Fd5 磷酸化受 SpkG 基因前一个基因 slr0151 编码的蛋白影响。我们提出 Slr0151 作为调节 Fd5 磷酸化和非磷酸化形式之间比例的辅助蛋白发挥作用。
