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PXD011805

PXD011805 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleMycobacterium smegtatis phosphoproteomics LC-MS/MS
DescriptionProtein 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.
HostingRepositoryPRIDE
AnnounceDate2019-11-12
AnnouncementXMLSubmission_2019-11-12_15:57:18.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterHelen O'Hare
SpeciesList scientific name: Mycolicibacterium smegmatis MKD8; NCBI TaxID: 1214915;
ModificationListphosphorylated residue
InstrumentLTQ Orbitrap Elite
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-11-23 01:20:44ID requested
12019-11-12 15:57:20announced
Publication List
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]
Keyword List
curator keyword: Biological
submitter keyword: bacterial protein phosphatase, bacterial signal transduction, phosphoproteomics, cell division, actinobacteria, mycobacteria, Mycobacterium smegmatis
Contact List
Dr Helen O'Hare
contact affiliationUniversity of Leicester, Department of Infection, Immunity & Inflammation and Molecular and Cell Biology, United Kingdom
contact emailhmo7@le.ac.uk
lab head
Helen O'Hare
contact affiliationUniversity of Leicester
contact emailhmo7@le.ac.uk
dataset submitter
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Dataset FTP location
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