Identifying and characterising Thrap3, Bclaf1 and Erh interactions using cross-linking mass spectrometry.

ABSTRACT: Background: Cross-linking mass spectrometry (XL-MS) is a powerful technology capable of yielding structural insights across the complex cellular protein interaction network. However, up to date most of the studies utilising XL-MS to characterise individual protein complexes' topology have been carried out on over-expressed or recombinant proteins, which might not accurately represent native cellular conditions. Methods: We performed XL-MS using MS-cleavable crosslinker disuccinimidyl sulfoxide (DSSO) after immunoprecipitation of endogenous BRG/Brahma-associated factors (BAF) complex and co-purifying proteins. Data are available via ProteomeXchange with identifier PXD027611. Results: Although we did not detect the expected enrichment of crosslinks within the BAF complex, we identified numer

SUBMITTER: Shcherbakova L 

PROVIDER: S-EPMC9270653 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature