Fig. 6: K1268-polyubiquitination of Rpb1 and the UBD of CSB strengthen the contacts of VHS with the p62 PH domain and K414-ubiquitinated UVSSA to enable TFIIH recruitment. | Nature Communications

Fig. 6: K1268-polyubiquitination of Rpb1 and the UBD of CSB strengthen the contacts of VHS with the p62 PH domain and K414-ubiquitinated UVSSA to enable TFIIH recruitment.

From: Molecular model of TFIIH recruitment to the transcription-coupled repair machinery

Fig. 6: K1268-polyubiquitination of Rpb1 and the UBD of CSB strengthen the contacts of VHS with the p62 PH domain and K414-ubiquitinated UVSSA to enable TFIIH recruitment.The alt text for this image may have been generated using AI.

a Integrative model of the TCR–TFIIH–Ub complex shown in surface representation. The three ubiquitin moieties in the model are colored as follows: Ub1 in olive, Ub2 in green, and Ub3 in medium purple. The UBD is shown in magenta, the UVSSA VHS domain in purple. The PH domain of p62 is in light green, and TFIIH is depicted in orange. b Zoomed-in view of Ub1, Ub2, and Ub3 interacting with Pol II Rpb1, Rpb9, the UBD of CSB, PHD, and UVSSA VHS domain. The sites of ubiquitin conjugation, Rpb1-K1268, and UVSSA-K414, are shown as van-der-Waals spheres. c Zoomed-in view of Ub1 conjugated to the K1268 site on Rpb1. d the CSB UBD interacting with the K48-linked Ub1 and Ub2. Key structural elements and residues at the interfaces are labeled and colored by domain. e Ub3 is conjugated to K414 on UVSSA and interacts with the p62 PH domain and UVSSA. f Interaction between the PHD, the TIR, and the VHS domain of UVSSA.

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