Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges.

ABSTRACT: Linker histone H1 (H1) is an abundant chromatin-binding protein that acts as an epigenetic regulator binding to nucleosomes and altering chromatin structures and dynamics. Nonetheless, the mechanistic details of its function remain poorly understood. Recent work suggest that the number and position of charged side chains on the globular domain (GD) of H1 influence chromatin structure and hence gene repression. Here, we solved the solution structure of the unbound GD of human H1.0, revealing that the structure is almost completely unperturbed by complex formation, except for a loop connecting two antiparallel β-strands. We further quantified the role of the many positive charges of the GD for its structure and conformational stability through the analysis of 11 charge variants. We find that

SUBMITTER: Martinsen JH 

PROVIDER: S-EPMC8927875 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature