Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division.

ABSTRACT: Protein phosphatase PstP is conserved throughout the Actinobacteria in a genetic locus related to cell wall synthesis and cell division. In many Actinobacteria it is the sole annotated serine threonine protein phosphatase to counter the activity of multiple serine threonine protein kinases. We used transcriptional knockdown, electron microscopy and comparative phosphoproteomics to investigate the putative dual functions of PstP as a specific regulator of cell division and as a global regulator of protein phosphorylation. Comparative phosphoproteomics in the early stages of PstP depletion showed hyperphosphorylation of protein kinases and their substrates, confirming PstP as a negative regulator of kinase activity and global serine and threonine phosphorylation. Analysis of the 838 phosphor

SUBMITTER: Iswahyudi 

PROVIDER: S-EPMC6554272 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature