MOESM2 of Internal modifications in the CENP-A nucleosome modulate centromeric dynamics

Additional file 2: Fig. S1. RMSF of proteins. A) This decrease in RMSF of Cα residues upon acetylation is more pronounced on the histone heterotetramer adjacent to the entry DNA. Of particular interest, the RMSF of the acetylated H2A acidic patch was suppressed with acetylation by −1 Å, and suppression is shown in the CENP-A C-terminus. The greater similarity shown in the RMSF of the reciprocal histones—CENP-A′, H4′. H2A′, and H2B′—could potentially be explained by the observed asymmetric unwrapping of DNA where the exit end in both systems dissociates to a similar amount (Fig. 3A). B) The RMSF of whole base pairs is shown for each DNA strand. Regions marked by I are DNA wrapped near the entry or near CENP-A and II are near the exit end of CENP-A′. The pseudo-dyad is marked by the vertical dotted line.