Role of Histone Tails in Structural Stability of the Nucleosome
Figure 12
Destabilization of H2A docking domain interaction with Ile51, Gln55 and the DNA upon H3 tail truncation.
(A) Interaction energy (vdw+electrostatics) between H2A docking domain and surrounding amino acids (B) Time series of the distance between the centers of mass of Ile51 or Gln55 and the nearest residue on the H2A C terminus (Leu115 and Asn110, respectively) is plotted. (C) Destabilization of H2A C terminus interaction with DNA upon H3 tail truncation. Time series of the minimum distance between Lys118 and Lys119 of H2A C terminus and the DNA is plotted. An increase of the distance between the C terminus end (Lys118 and Lys119) and DNA was considered to be a detachment if the minimum atomic distance between them during a tail-truncated simulation was greater than the minimum distance averaged over the intact nucleosome trajectory plus its standard deviation. The black line (dotted) indicates the minimum distance between C terminus and the DNA ( Å) below which the C terminus is ‘in contact’ with the DNA.