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

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...

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Published inJournal 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
LanguageEnglish
Published England Elsevier Ltd 22.02.2008
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Abstract 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. Eukaryotic XPB has only very limited helicase activity in vitro and may function as a DNA-dependent molecular switch to catalyse local distortion of DNA in transcription and repair. Most archaea have one or two homologues of the XPB protein with a presumed role in DNA repair, but only one other subunit of the TFIIH complex, the 5′–3′ helicase XPD, has been identified in archaea. Here we report the biochemical characterisation of the two homologous XPB proteins from the crenarchaeon Sulfolobus solfataricus. Although both proteins are single-stranded-DNA-stimulated ATPases, neither displays any helicase activity in vitro, consistent with recent studies of eukaryotic XPB. In almost all archaeal genomes, the xpb gene lies adjacent to a conserved partner gene, and we demonstrate that these two gene products form a physical interaction in vitro. We propose the name Bax1 ( Binds archaeal XPB) for this protein, which has a predicted endonuclease domain. XPB and Bax1 may collaborate in processing nucleic acid in an archaeal-specific DNA repair pathway.
AbstractList 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. Eukaryotic XPB has only very limited helicase activity in vitro and may function as a DNA-dependent molecular switch to catalyse local distortion of DNA in transcription and repair. Most archaea have one or two homologues of the XPB protein with a presumed role in DNA repair, but only one other subunit of the TFIIH complex, the 5'-3' helicase XPD, has been identified in archaea. Here we report the biochemical characterisation of the two homologous XPB proteins from the crenarchaeon Sulfolobus solfataricus. Although both proteins are single-stranded-DNA-stimulated ATPases, neither displays any helicase activity in vitro, consistent with recent studies of eukaryotic XPB. In almost all archaeal genomes, the xpb gene lies adjacent to a conserved partner gene, and we demonstrate that these two gene products form a physical interaction in vitro. We propose the name Bax1 (Binds archaeal XPB) for this protein, which has a predicted endonuclease domain. XPB and Bax1 may collaborate in processing nucleic acid in an archaeal-specific DNA repair pathway.
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. Eukaryotic XPB has only very limited helicase activity in vitro and may function as a DNA-dependent molecular switch to catalyse local distortion of DNA in transcription and repair. Most archaea have one or two homologues of the XPB protein with a presumed role in DNA repair, but only one other subunit of the TFIIH complex, the 5′–3′ helicase XPD, has been identified in archaea. Here we report the biochemical characterisation of the two homologous XPB proteins from the crenarchaeon Sulfolobus solfataricus. Although both proteins are single-stranded-DNA-stimulated ATPases, neither displays any helicase activity in vitro, consistent with recent studies of eukaryotic XPB. In almost all archaeal genomes, the xpb gene lies adjacent to a conserved partner gene, and we demonstrate that these two gene products form a physical interaction in vitro. We propose the name Bax1 ( Binds archaeal XPB) for this protein, which has a predicted endonuclease domain. XPB and Bax1 may collaborate in processing nucleic acid in an archaeal-specific DNA repair pathway.
Author Liu, Huanting
Roberts, Jennifer
White, Malcolm F.
Richards, Jodi D.
Cubeddu, Liza
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Issue 3
Keywords RT
transcription
EMSA
NER
Mes
XPB
helicase
CP
DNA repair
ssDNA
dsDNA
archaea
Language English
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SSID ssj0005348
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Snippet 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...
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...
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SubjectTerms 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
Title The Archaeal XPB Protein is a ssDNA-Dependent ATPase with a Novel Partner
URI https://dx.doi.org/10.1016/j.jmb.2007.12.019
https://www.ncbi.nlm.nih.gov/pubmed/18177890
https://search.proquest.com/docview/20889986
https://search.proquest.com/docview/70273056
Volume 376
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