PXD059817

PXD059817 is an original dataset announced via ProteomeXchange.

Title	Composition and liquid-to-solid maturation of protein aggregates contribute to bacterial dormancy development and recovery
Description	This study investigates the role of protein aggregation in bacterial dormancy in Escherichia coli (E. coli), with a focus on energy-related proteins. The research demonstrates how protein aggregation leads to ATP depletion and induces dormancy, with aggregates transitioning from liquid-like condensates to solid aggregates. The study shows that the dynamics of protein aggregation, particularly the solidification of aggregates, are key to the transition from the persister state to the viable-but-nonculturable (VBNC) state, impeding recovery. Chaperone DnaK is shown to play a central role in modulating aggregation and disaggregation. These findings offer insights into bacterial survival mechanisms, including chronic infections and antibiotic resistance, with implications for targeting dormant bacterial populations. Proteomics data supporting these conclusions are included for further exploration.
HostingRepository	PRIDE
AnnounceDate	2025-01-27
AnnouncementXML	Submission_2025-01-27_03:21:33.117.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD059817
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Ladan Khodaparast
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	amidated residue; acetylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-15 06:11:24	ID requested
⏵ 1	2025-01-27 03:21:33	announced

10.1038/S41467-025-56387-8;

10.6019/PXD059817;

submitter keyword: Bacterial Dormancy/ Protein Aggregation/ Energy Depletion (ATP)/ Liquid-to-Solid Phase Transition

Prof. Jan Michiels
contact affiliation	1 Centre of Microbial and Plant Genetics; KU Leuven; Leuven, 3000; Belgium 2 Center for Microbiology; VIB-KU Leuven; Leuven, 3000; Belgium
contact email	jan.michiels@kuleuven.be
lab head
Ladan Khodaparast
contact affiliation	Switch Laboratory at VIB-KU Leuven
contact email	Ladan.khodaparast@kuleuven.be
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/2025/01/PXD059817

PRIDE project URI

• PRIDE
  1. PXD059817
     1. Label: PRIDE project
     2. Name: Composition and liquid-to-solid maturation of protein aggregates contribute to bacterial dormancy development and recovery