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PXD001264

PXD001264 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleBacterial phosphoproteome
DescriptionProtein phosphorylation is a crucial post-translational modification in bacteria, but has not been extensively studied because of the technical difficulty of phosphopeptide enrichment. We present a new enrichment protocol, approximately 10 times more efficient than conventional approaches in E. coli. This protocol also performed well in B. subtilis and K. pneumoniae, in terms of high coverage and phosphopeptide identification numbers. Moreover, three high-confidence Ser/Thr phosphorylation motifs as well as 29 other motifs at various confidence levels were discovered for the first time, implying that both the position of phospho-acceptor residues and the surrounding sequences are critical for kinase-substrate specificity. As for N-terminal phosphorylation, a low rate of co-occurrence of N-terminal acetylation and acidic residues at the antepenultimate position appears to be prokaryote-specific. The comprehensive prokaryotic phosphoproteomes generated by our new protocol suggest the existence of distinct phosphorylation preferences between prokaryotes and eukaryotes.
HostingRepositoryPRIDE
AnnounceDate2015-09-22
AnnouncementXMLSubmission_2015-09-22_06:46:03.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMiao-Hsia Lin
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListphosphorylated residue
InstrumentTripleTOF 5600
Dataset History
RevisionDatetimeStatusChangeLog Entry
02014-08-26 01:45:36ID requested
12015-09-22 06:46:04announced
Publication List
Lin MH, Sugiyama N, Ishihama Y, Systematic profiling of the bacterial phosphoproteome reveals bacterium-specific features of phosphorylation. Sci Signal, 8(394):rs10(2015) [pubmed]
Keyword List
curator keyword: Biological, Technical
submitter keyword: Protein phosphorylation, LC-MS/MS
Contact List
Miao-Hsia Lin
contact affiliationDe[artment of Molecular and Cellular Bioanalysis, Graduate School of Pharmaceutical Sciences, Kyoto University
contact emailmiaohsialin@gmail.com
lab head
Miao-Hsia Lin
contact affiliationDepartment of Molecular and Cellular Bioanalysis, Graduate School of Pharmaceutical Sciences, Kyoto University, Japan
contact emailmiaohsialin@gmail.com
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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