Interplay of SpkG kinase and the Slr0151 protein in the phosphorylation of ferredoxin 5 in Synechocystis sp. strain PCC 6803

FEBS Lett. 2018 Feb;592(3):411-421. doi: 10.1002/1873-3468.12970. Epub 2018 Feb 1.

Abstract

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.

Keywords: S/T phosphorylation; SpkG protein kinase; ferredoxin 5 phosphoprotein.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Cyclic GMP-Dependent Protein Kinases / metabolism*
  • Ferredoxins / chemistry
  • Ferredoxins / metabolism*
  • Gene Knockout Techniques
  • Models, Molecular
  • Phosphorylation
  • Photosystem II Protein Complex / genetics
  • Photosystem II Protein Complex / metabolism*
  • Protein Binding
  • Proteomics
  • Sequence Alignment
  • Synechocystis / genetics
  • Synechocystis / metabolism*

Substances

  • 2Fe-2S ferredoxin
  • Bacterial Proteins
  • Ferredoxins
  • Photosystem II Protein Complex
  • Cyclic GMP-Dependent Protein Kinases