A Conserved G4 DNA Binding Domain in RecQ Family Helicases

RecQ family helicases play important roles at G-rich domains of the genome, including the telomeres, rDNA, and immunoglobulin switch regions. This appears to reflect the unusual ability of enzymes in this family to unwind G4 DNA. How RecQ family helicases recognize this substrate has not been establ...

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Veröffentlicht in:	Journal of molecular biology 2006-05, Vol.358 (4), p.1071-1080
Hauptverfasser:	Huber, Michael D., Duquette, Michelle L., Shiels, Jerome C., Maizels, Nancy
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Base Sequence Binding Sites - genetics Bloom syndrome cancer Conserved Sequence DNA - chemistry DNA - genetics DNA - metabolism DNA binding domain DNA Helicases - chemistry DNA Helicases - genetics DNA Helicases - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism G-quadruplex genomic instability Humans In Vitro Techniques Kinetics Microscopy, Electron Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RecQ Helicases Substrate Specificity
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