Proteomics

Dataset Information

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Immunoprecipitation-Mass Spectrometry (IP-MS) identifies components of a Mce4A-containing complex


ABSTRACT: How lipids travel between membranes of diderm bacteria is a challenging mechanistic question because lipids, which are hydrophobic molecules, must traverse a hydrophilic periplasm. This question is even more complex for mycobacteria, which have a unique cell envelope that is highly impermeable to molecules. A growing body of knowledge identifies Mce transporters as lipids importers for mycobacteria. Here, using protein stability experiments and immunoprecipitation-mass spectrometry to identify protein interactions among components of the mycobacterial Mce4 transporter we provide evidence for Mce transporters existing as multiprotein complexes.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mycobacterium Smegmatis (strain Atcc 700084 / Mc(2)155)

SUBMITTER: Laura Herring  

LAB HEAD: Miriam Braunstein

PROVIDER: PXD023082 | Pride | 2022-02-16

REPOSITORIES: Pride

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Publications

Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.

Rank Laura L   Herring Laura E LE   Braunstein Miriam M  

Journal of bacteriology 20210421 10


Mycobacteria possess Mce transporters that import lipids and are thought to function analogously to ATP-binding cassette (ABC) transporters. However, whereas ABC transporters import substrates using a single solute-binding protein (SBP) to deliver a substrate to permease proteins in the membrane, mycobacterial Mce transporters have a potential for six SBPs (MceA to MceF) working with a pair of permeases (YrbEA and YrbEB), a cytoplasmic ATPase (MceG), and multiple Mce-associated membrane (Mam) an  ...[more]

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