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Title: Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division.
Authors: Iswahyudi
Mukamolova, GV
Straatman-Iwanowska, AA
Allcock, N
Ajuh, P
Turapov, O
O'Hare, HM
First Published: 6-Jun-2019
Publisher: Nature Research (part of Springer Nature)
Citation: Scientific Reports, 2019, 9, Article number: 8337
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 phosphorylation sites that changed significantly, suggested that PstP may regulate diverse phosphoproteins, preferentially at phosphothreonine near acidic residues, near the protein termini, and within membrane associated proteins. Increased phosphorylation of the activation loop of protein kinase B (PknB) and of the essential PknB substrate CwlM offer possible explanations for the requirement for pstP for growth and for cell wall defects when PstP was depleted.
DOI Link: 10.1038/s41598-019-44841-9
eISSN: 2045-2322
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2019. This is an open-access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: The datasets generated during the current study are available in PRIDE, accession number: PXD011805.
Appears in Collections:Published Articles, Dept. of Infection, Immunity and Inflammation

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