Proteomics

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CobB interacting proteins identified by SPIDER assay

ABSTRACT: To assess whether SPIDER could detect transient interactions such as enzymes and their substrates, we examined the interactome of the E. coli protein deacetylase CobB. As the only member of the Sir2 family of deacetylases in E. coli, CobB is known to play a role in many different pathways but their interactors is still incompletely known. Here we applied SPIDER assay and a SILAC-based mass spectrometry strategy to capture and identify CobB Substrates. Biotinylated CobB was incubated with E. coli total lysate labeled with heavy stable isotope. As a control, free biotin was incubated with E. coli total lysate labeled with light stable isotope.

ORGANISM(S): Escherichia Coli

SUBMITTER: Shengce Tao  

PROVIDER: PXD026514 | iProX | Fri Jun 04 00:00:00 BST 2021

REPOSITORIES: iProX

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Protein-biomolecule interactions play pivotal roles in almost all biological processes. For a biomolecule of interest, the identification of the interacting protein(s) is essential. For this need, although many assays are available, highly robust and reliable methods are always desired. By combining a substrate-based proximity labeling activity from the pupylation pathway of Mycobacterium tuberculosis and the streptavidin (SA)-biotin system, we developed the Specific Pupylation as IDEntity Repor  ...[more]

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