PXD006195

PXD006195 is an original dataset announced via ProteomeXchange.

Title	Super-SILAC reveals intricate crosstalk between lipopolysaccharide, phospholipid and fatty acid metabolism in Escherichia coli
Description	The only membrane-anchored and essential ATP-dependent protease in Escherichia coli is FtsH. It controls the intracellular concentration of the deacetylase LpxC, which catalyses the first committed step in lipopolysaccharide biosynthesis. LpxC stability is strictly regulated in a growth rate-dependent manner to ascertain a vital equilibrium of lipopolysaccharide (LPS) and phospholipid biosynthesis. Previous studies suggested the involvement of yet unknown factors in LpxC degradation. Aiming at the identification of such factors that are predicted to be associated with LpxC and/or FtsH at high and low growth rates, we established a quantitative super-SILAC LC-MS/MS-based approach. The identification of known LpxC and FtsH interactors validated our approach. Several enzymes involved in fatty acid biosynthesis and degradation, including the central regulator FadR, interacted with LpxC and/or FtsH and showed a significant impact on LpxC stability. The newly identified LpxC and FtsH interactor WaaH, a LPS-modifying enzyme, stimulates LpxC degradation. Our results go beyond the previously established link between LPS and phospholipid biosynthesis and uncover a far-reaching network that controls LPS biosynthesis by involving multiple enzymes in fatty acid metabolism and phospholipid biosynthesis and modification.
HostingRepository	PRIDE
AnnounceDate	2019-11-12
AnnouncementXML	Submission_2019-11-12_11:58:26.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Katalin Barkovits
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	6x(13)C labeled residue; monohydroxylated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2017-03-29 00:50:36	ID requested
⏵ 1	2019-11-12 11:58:28	announced

Thomanek N, Arends J, Lindemann C, Barkovits K, Meyer HE, Marcus K, Narberhaus F, Modulates Proteolysis of LpxC. Front Microbiol, 9():3285(2018) [pubmed]

curator keyword: Biological

submitter keyword: LC-MS/MS, super-SILAC, quantitative proteomics, lipopolysaccharide, proteolysis, LpxC, FtsH, Escherichia coli

Katrin Marcus
contact affiliation	Ruhr-Universität Bochum Medizinische Proteom-Center Zentrum für klinische Forschung (ZKF) Raum 1.055 Universitätsstraße 150 44801 Bochum Germany
contact email	katrin.marcus@rub.de
lab head
Katalin Barkovits
contact affiliation	Ruhr University Bochum
contact email	katalin.barkovits@rub.de
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/2019/11/PXD006195

PRIDE project URI

• PRIDE
  1. PXD006195
     1. Label: PRIDE project
     2. Name: Super-SILAC reveals intricate crosstalk between lipopolysaccharide, phospholipid and fatty acid metabolism in Escherichia coli