Impact of inherent biases built into proteomic techniques: Proximity labeling and affinity capture compared.

ABSTRACT: The characterization of protein-protein interactions (PPIs) is of high value for understanding protein function. Two strategies are popular for identification of PPIs direct from the cellular environment: affinity capture (pulldown) isolates the protein of interest with an immobilized matrix that specifically captures the target and potential partners, whereas in BioID, genetic fusion of biotin ligase facilitates proximity biotinylation, and labeled proteins are isolated with streptavidin. Whilst both methods provide valuable insights, they can reveal distinct PPIs, but the basis for these differences is less obvious. Here, we compare both methods using four different trypanosome proteins as baits: poly(A)-binding proteins PABP1 and PABP2, mRNA export receptor MEX67, and the nucleoporin NU

SUBMITTER: Moreira CMDN 

PROVIDER: S-EPMC9791439 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature