PXD001979

PXD001979 is an original dataset announced via ProteomeXchange.

Title	Whole lysate and ribosome enriched fractions analyses of the amino terminal status of Escherichia coli at the steady state and upon deformylation inhibition
Description	A 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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:23:10.514.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Willy Bienvenut
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	N-formyl-L-methionine (Met); acetylated residue; monohydroxylated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2015-03-26 02:57:14	ID requested
1	2015-07-21 13:47:22	announced
⏵ 2	2024-10-22 04:23:18	announced	2024-10-22: Updated project metadata.

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]

10.1002/pmic.201500027;

curator keyword: Biological

submitter keyword: formylation/post-translational modifications/actinonin/acetylation/antibiotics

Willy V Bienvenut
contact affiliation	Institute 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 email	willy.bienvenut@isv.cnrs-gif.fr
lab head
Willy Bienvenut
contact affiliation	CNRS
contact email	willy.bienvenut@universite-paris-saclay.fr
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/2015/07/PXD001979

PRIDE project URI

• PRIDE
  1. PXD001979
     1. Label: PRIDE project
     2. Name: Whole lysate and ribosome enriched fractions analyses of the amino terminal status of Escherichia coli at the steady state and upon deformylation inhibition