Ontology highlight
ABSTRACT: Background
Histone H1 is involved in the formation and maintenance of chromatin higher order structure. H1 has multiple isoforms; the subtypes differ in timing of expression, extent of phosphorylation and turnover rate. In vertebrates, the amino acid substitution rates differ among subtypes by almost one order of magnitude, suggesting that each subtype might have acquired a unique function. We have devised a competitive assay to estimate the relative binding affinities of histone H1 mammalian somatic subtypes H1a-e and H1 degrees for long chromatin fragments (30-35 nucleosomes) in physiological salt (0.14 M NaCl) at constant stoichiometry.Results
The H1 complement of native chromatin was perturbed by adding an additional amount of one of the subtypes. A certain amount of SA
SUBMITTER: Orrego M
PROVIDER: S-EPMC1890542 | biostudies-literature | 2007 May
REPOSITORIES: biostudies-literature