The Archaeal XPB Protein is a ssDNA-Dependent ATPase with a Novel Partner

• Published in: Journal of molecular biology Vol. 376; no. 3; pp. 634 - 644
• Main Authors: Richards, Jodi D., Cubeddu, Liza, Roberts, Jennifer, Liu, Huanting, White, Malcolm F.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 22.02.2008
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - isolation & purification; Adenosine Triphosphatases - metabolism; Archaea; Archaeal Proteins - chemistry; Archaeal Proteins - genetics; Archaeal Proteins - isolation & purification; Archaeal Proteins - metabolism; DNA Repair; helicase; Protein Binding; Sulfolobus solfataricus; Sulfolobus solfataricus - chemistry; Sulfolobus solfataricus - genetics; Sulfolobus solfataricus - metabolism; transcription; XPB; RT; transcription; EMSA; NER; Mes; XPB; helicase; CP; DNA repair; ssDNA; dsDNA; archaea

XPB is a superfamily 2 helicase with a 3′–5′ polarity. In eukaryotes, XPB is an integral subunit of the transcription factor TFIIH, which plays a dual role in DNA opening at RNA polymerase II promoters and in establishing the repair bubble around a DNA lesion in nucleotide excision repair. Eukaryoti...