Fig. 4: TFIIH–nucleosome contacts. | Nature Structural & Molecular Biology

Fig. 4: TFIIH–nucleosome contacts.

From: Structures of transcription preinitiation complex engaged with the +1 nucleosome

Fig. 4

a, TFIIH–nucleosome interface in complex A. Tfb2 residues K495, K506 and R507, and Tfb5 residues R3, R5 and K6 from the dimerization domain contact DNA around the nucleosome dyad. Except for K495 in Tfb2, these TFIIH residues are conserved in human TFIIH. b, TFIIH–nucleosome interface in complex B. Four TFIIH subunits that are implicated in nucleosome contacts are shown in different colors. The view is related to the front view in Fig. 2a. The first contact may involve Ssl2 residue D103 and H3 residue R52. The second contact may involve Tfb2 residue K262 and the acidic patch on histones H2A and H2B. The third contact may involve Ssl1 residues K414, K417 and K420 that contact DNA around the nucleosome dyad. The fourth contact may involve Tfb4 residue R104 and histone H4 residue D24. Except for R104 in Tfb4 and K414 and K417 in Ssl1, these TFIIH residues are conserved in human TFIIH.

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