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PXD014436

PXD014436 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleConserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome
DescriptionThe physiological role of LepA, a paralog of EF-G found in all bacteria, has been a mystery for decades. Here, we show that LepA functions in ribosome biogenesis. In cells lacking LepA, immature 30S particles accumulate. Four proteins are specifically underrepresented in these particles-S3, S10, S14, and S21-all of which bind late in the assembly process and contribute to the folding of the 3' domain of 16S rRNA. Processing of 16S rRNA is also delayed in the mutant strain, as indicated by increased levels of precursor 17S rRNA in assembly intermediates. Mutation ΔlepA confers a synthetic growth phenotype in absence of RsgA, another GTPase, well known to act in 30S subunit assembly. Analysis of the ΔrsgA strain reveals accumulation of intermediates that resemble those seen in the absence of LepA. These data suggest that RsgA and LepA play partially redundant roles to ensure efficient 30S assembly. This data is published in paper PMID: 28096346
HostingRepositoryPRIDE
AnnounceDate2019-07-03
AnnouncementXMLSubmission_2019-07-03_07:47:42.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJenny Moon
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListNo PTMs are included in the dataset
InstrumentBruker Daltonics instrument model
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-07-01 01:39:25ID requested
12019-07-03 07:47:43announced
Publication List
Gibbs MR, Moon KM, Chen M, Balakrishnan R, Foster LJ, Fredrick K, Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome. Proc Natl Acad Sci U S A, 114(5):980-985(2017) [pubmed]
Keyword List
submitter keyword: EF4
RsgA
YjeQ
protein synthesis
translation
Contact List
Leonard J. Foster
contact affiliationBiochemistry and Molecular Biology, Michael Smith Laboratories, University of British Columbia, Canada
contact emailfoster@msl.ubc.ca
lab head
Jenny Moon
contact affiliationUniversity of British Columbia
contact emailkyungmee@mail.ubc.ca
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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