|
Figure 4.
Figure 4. Details of Eaf3 Chromo Barrel Domain Interaction
with the Linked Histone H3K[C]36me2 Sequence
(A) Chemical
conversion of a cysteine residue to a dimethyllysine analog
(K[C]me2).
(B) Close-up view of the main interaction site
within the Eaf3-H3K[C]36me2 protein. Tyr23, Tyr81, Trp84, and
Trp88 of the chromo barrel domain of Eaf3 form an aromatic cage
that accommodates the linked dimethylated lysine analog of
H3K36. Other residues (Leu21 and Lys85 of Eaf3; and V35 and
Pro38 of linked H3K[C]36me2) involved in the interaction are
also labeled.
(C) Planes from the 3D ^15N nuclear
Overhauser effect spectroscopy (NOESY) experiment showing NOE
correlations of W88HE1 of Eaf3 to K[C]36me2, Lys37, and Pro38 of
linked H3K[C]36me2 (left); and ^13C-edited NOESY experiments
showing NOE correlations of W88HE3 of Eaf3 to K[C]36me2, Lys37,
and Pro38 of linked H3K[C]36me2 (middle), and NOE correlations
of the HD protons of P38 of linked H3K[C]36me2 to the aromatic
protons of Trp84 and Trp88 of Eaf3 (right).
(D) Stereo view
of the superposition of 10 NMR structures each of free Eaf3
(blue) and Eaf3-H3K[C]36me2 complex (Eaf3 in green and
H3K[C]36me2 in orange) showing a close-up representation of the
aromatic pocket binding site.
|
