PXD035239

PXD035239 is an original dataset announced via ProteomeXchange.

Title	Lysine trimethylation in planktonic and pellicle modes of growth in Acinetobacter baumannii
Description	An increasing number of studies have shown the importance of post-translational modifications (PTM) in bacterial physiology, especially during biofilm formation. Trimethylation of lysine residues is little studied due to lack of specific enrichment methods for this PTM. However, it may have a significant role in virulence, adaptation or biofilm formation. Acinetobacter baumannii has been described as an important nosocomial pathogen over the past 30 years, frequently implicated in ventilator-associated infections. Many aspects of the biology of A. baumannii remain elusive, in particular the formation of an air-liquid biofilm (pellicle). Here, we investigated K-trimethylation in A. baumannii ATCC 17978 in planktonic and pellicle modes by proteomic analysis, using different analytical approaches. Here, we identified 84 K-trimethylated proteins. Among these proteins, several are localized to the membrane or involved in adhesion, biofilm formation, lipid metabolism and even characterized as virulence or resistance factors. Our results confirmed some K-trimethylated sites previously identified in other bacteria, such as three sites on the 50S ribosomal subunit protein L11 (RplK). But we also identified novel sites such as K1020 on the adhesin Ata autotransporter (Ata), which is a known virulence factor and participates in bacterial adhesion. Overall, this study is the first large-scale proteomic study of trimethylation in A. baumannii and will be an important resource for the scientific community.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:03:57.111.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julie Hardouin
SpeciesList	scientific name: Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377); NCBI TaxID: 400667;
ModificationList	monomethylated residue; acetylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2022-07-11 08:29:07	ID requested
1	2023-07-20 12:55:08	announced
⏵ 2	2023-11-14 09:04:04	announced	2023-11-14: Updated project metadata.

Nalpas N, Kentache T, D, é E, Hardouin J, . J Proteome Res, 22(7):2339-2351(2023) [pubmed]

submitter keyword: Acinetobacter baumannii, planktonic, lysine trimethylation, Proteomics, pellicle

Julie Hardouin
contact affiliation	Laboratoire Polymères, Biopolymères, Surfaces, UMR CNRS 6270, Université de Rouen, 76821 Mont-Saint-Aignan cedex, France
contact email	julie.hardouin@univ-rouen.fr
lab head
Julie Hardouin
contact affiliation	Université de Rouen - laboratoire PBS
contact email	julie.hardouin@univ-rouen.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD035239
     1. Label: PRIDE project
     2. Name: Lysine trimethylation in planktonic and pellicle modes of growth in Acinetobacter baumannii