Specific pupylation as IDEntity reporter (SPIDER) for the identification of protein-biomolecule interactions.
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ABSTRACT: 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 Reporter (SPIDER) method for identifying protein-biomolecule interactions. Using SPIDER, we validated the interactions between the known binding proteins of protein, DNA, RNA, and small molecule. We successfully applied SPIDER to construct the global protein interactome for m6A and mRNA, ident
SUBMITTER: Jiang HW
PROVIDER: S-EPMC10103678 | biostudies-literature | 2023 Apr
REPOSITORIES: biostudies-literature
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