Dataset Information

Global proteomic responses of Escherichia coli, Klebsiella pneumoniae, Enterococcus faecium and Staphylococcus aureus to sub-inhibitory concentrations of antibiotics using LC-MS/MS analysis

ABSTRACT: The objective of this study was to analyse proteomic profiles of antibiotic-susceptible E. coli MG1655, K. pneumoniae NCTC418, E. faecium NCTC13169, and S. aureus NCTC8325 under sub-inhibitory antibiotic stress. Gram-negative bacteria were exposed to cefotaxime, ciprofloxacin, kanamycin, and imipenem, while Gram-positive bacteria were treated with chloramphenicol, vancomycin, or oxacillin.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli Staphylococcus Aureus Bacteria Enterococcus Faecium Klebsiella Pneumoniae

TISSUE(S): Cell Culture

SUBMITTER: Monika Subanovic

LAB HEAD: Prof. Fiona Walsh

PROVIDER: PXD061388 | Pride | 2025-09-22

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	E_coli_cefotaxime_1.raw	Raw
	E_coli_cefotaxime_2.raw	Raw
	E_coli_cefotaxime_3.raw	Raw
	E_coli_cefotaxime_vs_control_SEARCH.zip	Other
	E_coli_ciprofloxacin_1.raw	Raw

Items per page:

1 - 5 of 61

Publications

Proteomic and metabolomic responses of priority bacterial pathogens to subinhibitory concentration of antibiotics.

Subanovic Monika M Frawley Dean D Tierney Ciara C Velasco-Torrijos Trinidad T Walsh Fiona F

npj antimicrobials and resistance 20250916 1

This study employed a comprehensive proteomic and metabolomic analysis to characterize adaptive cellular mechanisms of priority pathogens-Escherichia coli, Klebsiella pneumoniae, Enterococcus faecium, and Staphylococcus aureus-under sub-inhibitory concentrations of antibiotics. Despite significant metabolomic perturbations, some pathogens had minimal or no significant changes in their proteome. Notably, trimethylamine metabolism was consistently altered across all species, suggesting its role in ...[more]

PMID: 40957891

Similar Datasets

Project description:Maintaining the dynamic structure of chromatin is critical for regulating the cellular processes that require access to the DNA template, such as DNA damage repair, transcription, and replication. Histone chaperones and ATP-dependent chromatin remodeling factors facilitate transitions in chromatin structure by assembling and positioning nucleosomes through a variety of enzymatic activities. SMARCAD1 is a unique chromatin remodeler that combines the ATP-dependent ability to exchange histones, with the chaperone-like activity of nucleosome deposition. We have shown previously that phosphorylated SMARCAD1 exhibits reduced binding to nucleosomes. However, it is unknown how phosphorylation affects SMARCAD1’s ability to perform its various enzymatic activities. Here we use mutational analysis, activity assays, and mass spectrometry, to probe SMARCAD1 regulation and to investigate the role of its flexible N-terminal region. We show that phosphorylation affects SMARCAD1 binding to nucleosomes and DNA, as well as ATP hydrolysis and histone exchange. Conversely, we report that phosphorylation is inconsequential for histone binding and nucleosome assembly. In addition, the SMARCAD1 N-terminal region is revealed to be critical for nucleosome assembly and histone exchange. Together, this work examines the intricacies of how phosphorylation governs SMARCAD1 activity and provides insight into its complex regulation and diverse activities.Maintaining the dynamic structure of chromatin is critical for regulating the cellular processes that require access to the DNA template, such as DNA damage repair, transcription, and replication. Histone chaperones and ATP-dependent chromatin remodeling factors facilitate transitions in chromatin structure by assembling and positioning nucleosomes through a variety of enzymatic activities. SMARCAD1 is a unique chromatin remodeler that combines the ATP-dependent ability to exchange histones, with the chaperone-like activity of nucleosome deposition. We have shown previously that phosphorylated SMARCAD1 exhibits reduced binding to nucleosomes. However, it is unknown how phosphorylation affects SMARCAD1’s ability to perform its various enzymatic activities. Here we use mutational analysis, activity assays, and mass spectrometry, to probe SMARCAD1 regulation and to investigate the role of its flexible N-terminal region. We show that phosphorylation affects SMARCAD1 binding to nucleosomes and DNA, as well as ATP hydrolysis and histone exchange. Conversely, we report that phosphorylation is inconsequential for histone binding and nucleosome assembly. In addition, the SMARCAD1 N-terminal region is revealed to be critical for nucleosome assembly and histone exchange. Together, this work examines the intricacies of how phosphorylation governs SMARCAD1 activity and provides insight into its complex regulation and diverse activities.