Proteomics

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The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC in the cytoplasm of Shigella flexneri


ABSTRACT: Using TurboID to study the proxisome of Shigella flexneri's Type 3 Secretion System (T3SS) chaperone IpgC, and transcriptional activator MxiE. The proxisome was studied in the ON (active secretion) and OFF (inactive secretion) states of the T3SS using N and C -terminal fusions of TurboID to the baits IpgC and MxiE.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Shigella Flexneri 5a Str. M90t (ncbitaxon:1086030)

SUBMITTER: Francois-Xavier Campbell-Valois  

PROVIDER: MSV000095473 | MassIVE | Mon Jul 29 08:15:00 BST 2024

SECONDARY ACCESSION(S): PXD054349

REPOSITORIES: MassIVE

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The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC in <i>Shigella flexneri</i>.

Haidar-Ahmad Nathaline N   Tomaro Kyle K   Lavallée-Adam Mathieu M   Campbell-Valois François-Xavier F-X  

mSphere 20241031 11


Promiscuous biotin ligases derived from the bacterial enzyme BirA are used to identify proteins vicinal to a bait protein, thereby defining its proxisome. Despite the popularity of this approach, surprisingly little is known about its use in prokaryotes. Here, we compared the activity of four widely used promiscuous biotin ligases in the cytoplasm of <i>Shigella flexneri</i>, a pathogenic subgroup of <i>Escherichia coli</i>. Our data indicate that the kinetics of TurboID's biotinylating activity  ...[more]

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