Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division



Iswahyudi, , Mukamolova, Galina V, Straatman-Iwanowska, Anna A, Allcock, Natalie, Ajuh, Paul, Turapov, Obolbek and O'Hare, Helen M
(2019) Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division. SCIENTIFIC REPORTS, 9 (1). 8337-.

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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.

Item Type: Article
Uncontrolled Keywords: Cell Wall, Mycobacterium smegmatis, Mycobacterium tuberculosis, Bacterial Proteins, Phosphoproteins, Microscopy, Electron, Proteomics, Gene Expression Regulation, Bacterial, Phosphorylation, Mutation, Multigene Family, Computer Simulation, Promoter Regions, Genetic, Protein Serine-Threonine Kinases
Divisions: Faculty of Health and Life Sciences
Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User: Symplectic Admin
Date Deposited: 31 Mar 2022 07:39
Last Modified: 18 Jan 2023 21:06
DOI: 10.1038/s41598-019-44841-9
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3151771