Histone isoform H2A1H promotes attainment of distinct physiological states by altering chromatin dynamics.

ABSTRACT:

Background

The distinct functional effects of the replication-dependent histone H2A isoforms have been demonstrated; however, the mechanistic basis of the non-redundancy remains unclear. Here, we have investigated the specific functional contribution of the histone H2A isoform H2A1H, which differs from another isoform H2A2A3 in the identity of only three amino acids.

Results

H2A1H exhibits varied expression levels in different normal tissues and human cancer cell lines (H2A1C in humans). It also promotes cell proliferation in a context-dependent manner when exogenously overexpressed. To uncover the molecular basis of the non-redundancy, equilibrium unfolding of recombinant H2A1H-H2B dimer was performed. We found that the M51L alteration at the H2A-H2B dimer interface decreas

SUBMITTER: Bhattacharya S 

PROVIDER: S-EPMC5648446 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature