PXD011805

PXD011805 is an original dataset announced via ProteomeXchange.

Title	Mycobacterium smegtatis phosphoproteomics LC-MS/MS
Description	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. pstP knockdown in Mycobacterium smegmatis led to thickening of the cell wall and septum, changes in cell morphology, and eventual cell lysis. 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 have broad specificity, with preference for phosphothreonine, phosphosites 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 essentiality of pstP and the cell wall defects when PstP was depleted.
HostingRepository	PRIDE
AnnounceDate	2019-11-12
AnnouncementXML	Submission_2019-11-12_15:57:18.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Helen O'Hare
SpeciesList	scientific name: Mycolicibacterium smegmatis MKD8; NCBI TaxID: 1214915;
ModificationList	phosphorylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2018-11-23 01:20:44	ID requested
⏵ 1	2019-11-12 15:57:20	announced

Iswahyudi, Mukamolova GV, Straatman-Iwanowska AA, Allcock N, Ajuh P, Turapov O, O'Hare HM, Mycobacterial phosphatase PstP regulates global serine threonine phosphorylation and cell division. Sci Rep, 9(1):8337(2019) [pubmed]

curator keyword: Biological

submitter keyword: bacterial protein phosphatase, bacterial signal transduction, phosphoproteomics, cell division, actinobacteria, mycobacteria, Mycobacterium smegmatis

Dr Helen O'Hare
contact affiliation	University of Leicester, Department of Infection, Immunity & Inflammation and Molecular and Cell Biology, United Kingdom
contact email	hmo7@le.ac.uk
lab head
Helen O'Hare
contact affiliation	University of Leicester
contact email	hmo7@le.ac.uk
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/11/PXD011805

PRIDE project URI

• PRIDE
  1. PXD011805
     1. Label: PRIDE project
     2. Name: Mycobacterium smegtatis phosphoproteomics LC-MS/MS