This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain (PUBMED:16530788).
This entry represents the RQC domain, which is a DNA-binding domain found only in RecQ family enzymes. RecQ family helicases can unwind G4 DNA, and play important roles at G-rich domains of the genome, including the telomeres, rDNA, and immunoglobulin switch regions. This domain has a helix-turn-helix structure and acts as a high affinity G4 DNA binding domain [ (PUBMED:16530788) ]. Binding of RecQ to Holliday junctions involves both the RQC and the HRDC domains.
A conserved G4 DNA binding domain in RecQ family helicases.
J Mol Biol. 2006; 358: 1071-80
Display abstract
RecQ family helicases play important roles at G-rich domains of thegenome, including the telomeres, rDNA, and immunoglobulin switch regions.This appears to reflect the unusual ability of enzymes in this family tounwind G4 DNA. How RecQ family helicases recognize this substrate has notbeen established. Here, we show that G4 DNA is a preferred target for BLMhelicase within the context of long DNA molecules. We identify the RQCdomain, found only in RecQ family enzymes, as an independent, highaffinity and conserved G4 DNA binding domain; and show that binding toHolliday junctions involves both the RQC and the HRDC domains. Theseresults provide mechanistic understanding of differences and redundanciesof function and activities among RecQ family helicases, and of howdeficiencies in human members of this family may contribute to genomicinstability and disease.
