Protein disorder-to-order transition enhances the nucleosome-binding affinity of H1.

ABSTRACT: Intrinsically disordered proteins are crucial elements of chromatin heterogenous organization. While disorder in the histone tails enables a large variation of inter-nucleosome arrangements, disorder within the chromatin-binding proteins facilitates promiscuous binding to a wide range of different molecular targets, consistent with structural heterogeneity. Among the partially disordered chromatin-binding proteins, the H1 linker histone influences a myriad of chromatin characteristics including compaction, nucleosome spacing, transcription regulation, and the recruitment of other chromatin regulating proteins. Although it is now established that the long C-terminal domain (CTD) of H1 remains disordered upon nucleosome binding and that such disorder favours chromatin fluidity, the structura

SUBMITTER: Sridhar A 

PROVIDER: S-EPMC7261198 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature