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PXD001983

PXD001983 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state
DescriptionA proteome-wide analysis was performed in Escherichia coli to identify the impact on protein N-termini of the antibiotic actinonin specifically inhibiting peptide deformylase (PDF). A new strategy and tool suite (SILProNaQ) was employed to provide large scale N-terminus acetylation yield quantitation. In control conditions, more than 1000 N-termini could be identified with 56 % Met removal, and additional modifications involving partial or complete N-acetylation (10%) and formyl retention (5%). Among the proteins undergoing these N-terminal modifications, some translocated membrane proteins were highlighted. The early time-course impact of actinonin was followed after the addition of bacteriostatic concentrations of the drug immediately slowing down the growth rate. Under these conditions, 25% of all proteins remain formylated after 10 min, a value reaching more than 60% of all characterized proteins after 40 min of treatment. The N-formylation rate on individual proteins increased with the same trend. Upon PDF inhibition, we finally show that two major categories of proteins retain their formyl group: a large number of inner membrane proteins and proteins involved in protein synthesis including many factors assisting the nascent chains in co-translational events.
HostingRepositoryPRIDE
AnnounceDate2017-09-25
AnnouncementXMLSubmission_2017-09-25_01:03:44.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterWilly Bienvenut
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListacetate labeling reagent (N-term) (heavy form: +3amu); 3x(2)H labeled N6-acetyl-L-lysine; N-formyl-L-methionine (Met); monohydroxylated residue; acetylated residue
InstrumentLTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-03-26 09:07:58ID requested
12015-07-22 03:11:32announced
22017-09-25 01:03:46announcedUpdated publication reference for PubMed record(s): 28887476, 26017780.
Publication List
Bienvenut WV, Giglione C, Meinnel T, Proteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition. Proteomics, 15(14):2503-18(2015) [pubmed]
Grzela R, Nusbaum J, Fieulaine S, Lavecchia F, Bienvenut WV, Dian C, Meinnel T, Giglione C, The C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation. Sci Rep, 7(1):11041(2017) [pubmed]
Keyword List
curator keyword: Biological
submitter keyword: formylation/post-translational modifications/actinonin/acetylation/antibiotics
Contact List
Willy V Bienvenut
contact affiliationInstitute of Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Bâtiment 23A, 1 avenue de la Terrasse, F-91198 Gif-sur-Yvette cedex, France.
contact emailwilly.bienvenut@isv.cnrs-gif.fr
lab head
Willy Bienvenut
contact affiliationCNRS
contact emailwilly.bienvenut@isv.cnrs-gif.fr
dataset submitter
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Dataset FTP location
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