XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase

• Published in: DNA repair Vol. 10; no. 7; pp. 697 - 713
• Main Authors: Fuss, Jill O., Tainer, John A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 15.07.2011
• Subjects: Adenosine Triphosphate - metabolism; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Catalytic Domain; Cell Cycle; Cyclin-Dependent Kinases - genetics; Cyclin-Dependent Kinases - metabolism; DNA - genetics; DNA - metabolism; DNA Damage; DNA Repair; DNA Repair Enzymes - genetics; DNA Repair Enzymes - metabolism; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Helicase; Human disease; Humans; Models, Molecular; Nucleotide excision repair; Protein Structure, Tertiary; Signal Transduction; Structure; TFIIH assembly; Transcription Factor TFIIH - genetics; Transcription Factor TFIIH - metabolism; Transcription, Genetic; Xeroderma Pigmentosum - genetics; Xeroderma Pigmentosum - metabolism; Xeroderma Pigmentosum Group D Protein - genetics; Xeroderma Pigmentosum Group D Protein - metabolism; Helicase; Nucleotide excision repair; Human disease; TFIIH assembly; Structure

Helicases must unwind DNA at the right place and time to maintain genomic integrity or gene expression. 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 duple...