
Dynamic conformational switching underlies TFIIH function in ...
May 13, 2023 · Our study uncovers an internal regulatory mechanism that switches XPB and XPD activities making them mutually exclusive between NER and transcription initiation. By sequentially coordinating...
In TFIIH the Arch domain of XPD is mechanistically essential for ...
Apr 3, 2020 · Here we present the high-resolution crystal structure of the Arch domain of XPD with its interaction partner MAT1, a central component of the CDK activating kinase complex. The analysis of the...
The essential and multifunctional TFIIH complex - PMC
We describe the structure of TFIIH and its roles in pol II initiation, promoter‐proximal pausing, elongation, and termination. We also discuss cellular roles for TFIIH beyond transcription (e.g. DNA repair, cell cycle regulation) and summarize small molecule inhibitors of TFIIH and diseases associated with defects in TFIIH structure and function.
The complete structure of the human TFIIH core complex
Mar 12, 2019 · Greber et al. used an approach called cryo-electron microscopy (also called cryo-EM) to reveal the structure of TFIIH collected from human cells. The structure revealed several new details, including how p52 helps XPB attach to the rest of TFIIH, and that p62 helps to control the activity of XPD.
In TFIIH, XPD Helicase Is Exclusively Devoted to DNA Repair
Sep 30, 2014 · The eukaryotic XPD helicase is an essential subunit of TFIIH involved in both transcription and nucleotide excision repair (NER). Mutations in human XPD are associated with several inherited diseases such as xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy.
TFIIH: A multi-subunit complex at the cross-roads of ... - PubMed
Transcription factor IIH (TFIIH) is a multiprotein complex involved in both eukaryotic transcription and DNA repair, revealing a tight connection between these two processes. Composed of 10 subunits, it can be resolved into a 7-subunits core complex with the XPB translocase and the XPD helicase, and …
In TFIIH the Arch domain of XPD is mechanistically essential for ...
Apr 3, 2020 · Here we present the high-resolution crystal structure of the Arch domain of XPD with its interaction partner MAT1, a central component of the CDK activating kinase complex. The analysis of the interface led to the identification of amino acid residues that are crucial for the MAT1-XPD interaction.
XPB and XPD helicases in TFIIH orchestrate DNA duplex opening …
Jul 15, 2011 · Biologically critical XPB and XPD helicases are key members of the human TFIIH complex; they anchor CAK kinase (cyclinH, MAT1, CDK7) to TFIIH and open DNA for transcription and for repair of duplex distorting damage by nucleotide excision repair (NER).
XPD Mutations Prevent TFIIH-Dependent Transactivation by …
Apr 5, 2002 · Inherited mutations in the XPD subunit of the general transcription/repair factor TFIIH yield the rare genetic disorder Xeroderma pigmentosum (XP), the phenotypes of which cannot be explained solely on the basis of a DNA repair defect.
In TFIIH the Arch domain of XPD is mechanistically essential for ...
The XPD helicase is a central component of the general transcription factor TFIIH which plays major roles in transcription and nucleotide excision repair (NER). Here we present the high-resolution crystal structure of the Arch domain of XPD with its ...
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