PXD059040

PXD059040 is an original dataset announced via ProteomeXchange.

Title	Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization
Description	Many pathogenic bacteria use proteinaceous ethanolamine-utilization microcompartments (Eut BMCs) to facilitate the catabolism of ethanolamine, an abundant nutrient in the mammalian gut. The ability to metabolize ethanolamine gives pathogens a competitive edge over commensal microbiota which can drive virulence in the inflamed gut. Despite their critical functions, the molecular mechanisms underlying the synthesis of Eut BMCs in bacterial cells remain elusive. Here, we report a systematic study for dissecting the molecular basis underlying Eut BMC assembly in Salmonella. We determined the functions of individual constituent proteins in the structure and function of Eut BMCs and demonstrated that EutQ plays an essential role in both cargo encapsulation and Eut BMC formation through specific association with the shell and cargo enzymes. Furthermore, our data reveal that Eut proteins can self-assemble to form cargo and shell aggregates independently in vivo, and that the biogenesis of Eut BMCs follows a “Shell-first” pathway. Cargo enzymes exhibit dynamic liquid-like organization within the Eut BMC. These discoveries provide mechanistic insights into the structure and assembly of the Eut BMC, which serves as a paradigm for membrane-less organelles.
HostingRepository	PRIDE
AnnounceDate	2025-10-06
AnnouncementXML	Submission_2025-10-05_20:19:57.392.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Joscelyn Harris
SpeciesList	scientific name: Bacteria; NCBI TaxID: NCBITaxon:2; scientific name: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); NCBI TaxID: NEWT:99287;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	timsTOF HT

Revision	Datetime	Status	ChangeLog Entry
0	2024-12-19 01:59:08	ID requested
⏵ 1	2025-10-05 20:19:58	announced

Yang M, Adegbite O, Chang P, Cheng J, Wang Y, Held M, Zhu X, Li Y, Dykes GF, Chen Y, Savage N, Zhang YZ, Gao J, Hinton JCD, Lian LY, Liu LN, Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization. Sci Adv, 11(40):eadx9774(2025) [pubmed]

10.1126/sciadv.adx9774;

submitter keyword: salmonella

Lu-Ning Liu
contact affiliation	Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB United Kingdom MOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for 10 Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China.
contact email	luning.liu@liverpool.ac.uk
lab head
Joscelyn Harris
contact affiliation	University of Liverpool
contact email	jsarsby@liverpool.ac.uk
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/2025/10/PXD059040

PRIDE project URI

• PRIDE
  1. PXD059040
     1. Label: PRIDE project
     2. Name: Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization