Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex.

ABSTRACT: The multi-subunit nucleosome remodeling and deacetylase (NuRD) complex consists of seven subunits, each of which comprises two or three paralogs in vertebrates. These paralogs define mutually exclusive and functionally distinct complexes. In addition, several proteins in the complex are multimeric, which complicates structural studies. Attempts to purify sufficient amounts of endogenous complex or recombinantly reconstitute the complex for structural studies have proven quite challenging. Until now, only substructures of individual domains or proteins and low-resolution densities of (partial) complexes have been reported. In this study, we comprehensively investigated the relative orientation of different subunits within the NuRD complex using multiple cross-link IP mass spectrometry (xIP-

SUBMITTER: Spruijt CG 

PROVIDER: S-EPMC8246863 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature