PXD043277

PXD043277 is an original dataset announced via ProteomeXchange.

Title	Acetyl-proteome profiling of Staphylococcus aureus revealed lysine acetylation in bacterial antibiotic resistance
Description	Protein post-translational modifications (PTMs) play crucial roles in various biological processes across prokaryotes and eukaryotes. Lysine acetylation (Kac), which is observed in different bacteria species and is known to be a dynamic and reversible PTM involved in numerous physiological functions. However, limited research has been conducted to explore the connection between Kac and bacterial antibiotic resistance. In this investigation, we employed advanced 4D label-free quantitative proteomics technology to examine the differential expression of Kac-modified proteins in Staphylococcus aureus strains: one susceptible to erythromycin (Ery-S) and another induced to be resistant (Ery-R). Our systematic analysis identified a total of 1808 acetylated proteins with 6791 specific Kac sites. Notably, we quantified 1907 of these sites across 483 proteins. A total of 548 Kac sites were affected by erythromycin pressure on 316 acetylated proteins. Functional analyses uncovered a notable presence of differentially acetylated proteins (DAPs) within pathways associated with ribosome assembly, glycolysis, and lysine biosynthesis. Moreover, our findings indicate a significant acetylation of ribosomal proteins in antibiotic-resistant strains, implying a potential regulatory role of this modification in translation processes. Further investigations using polysome profiling experiments revealed that Kac modification of ribosomal and ribosome-associated proteins can maintain translation in response to antibiotic stress. Our data provides support for the link between protein lysine acetylation and bacterial antibiotic resistance, highlighting the potential involvement of ribosome translation. These findings collectively unveil a novel mechanism that enhances our understanding of bacterial antibiotic resistance and offer valuable insights for the development of antibiotic treatment strategies.
HostingRepository	PRIDE
AnnounceDate	2024-10-17
AnnouncementXML	Submission_2024-10-17_04:00:07.335.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Miao Feng
SpeciesList	scientific name: Staphylococcus aureus; NCBI TaxID: 1280;
ModificationList	acetylated residue
Instrument	timsTOF

Revision	Datetime	Status	ChangeLog Entry
0	2023-06-25 07:53:15	ID requested
⏵ 1	2024-10-17 04:00:08	announced

Feng M, Yi X, Feng Y, He F, Xiao Z, Yao H, . Heliyon, 10(15):e35326(2024) [pubmed]

10.1016/j.heliyon.2024.e35326;

submitter keyword: post-translational modification

Staphylococcus aureus

antibiotic resistance

lysine acetylation

ribosome

Miao Feng
contact affiliation	Capital Institute of Pediatrics
contact email	fengmiao3371@126.com
lab head
Miao Feng
contact affiliation	Capital Institute of Pediatrics
contact email	fengmiao3371@126.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043277
     1. Label: PRIDE project
     2. Name: Acetyl-proteome profiling of Staphylococcus aureus revealed lysine acetylation in bacterial antibiotic resistance