Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer.

ABSTRACT: The folding pathway of the histone H2A-H2B heterodimer minimally includes an on-pathway, dimeric, burst-phase intermediate, I(2). The partially folded H2A and H2B monomers populated at equilibrium were characterized as potential monomeric kinetic intermediates. Folding kinetics were compared for initiation from isolated, folded monomers and the heterodimer unfolded in 4 M urea. The observed rates were virtually identical above 0.4 M urea, exhibiting a log-linear relationship on the final denaturant concentration. Below approximately 0.4 M urea (concentrations inaccessible from the 4-M urea unfolded state), a rollover in the rates was observed; this suggests that a component of the I(2) ensemble contains non-native structure that rearranges/isomerizes to a more native-like species. The cont

SUBMITTER: Stump MR 

PROVIDER: S-EPMC2914809 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature