RECQL4 Promotes DNA End Resection in Repair of DNA Double-Strand Breaks

Cell Rep. 2016 Jun 28;16(1):161-173. doi: 10.1016/j.celrep.2016.05.079. Epub 2016 Jun 16.

Abstract

The RecQ helicase RECQL4, mutated in Rothmund-Thomson syndrome, regulates genome stability, aging, and cancer. Here, we identify a crucial role for RECQL4 in DNA end resection, which is the initial and an essential step of homologous recombination (HR)-dependent DNA double-strand break repair (DSBR). Depletion of RECQL4 severely reduces HR-mediated repair and 5' end resection in vivo. RECQL4 physically interacts with MRE11-RAD50-NBS1 (MRN), which senses DSBs and initiates DNA end resection with CtIP. The MRE11 exonuclease regulates the retention of RECQL4 at laser-induced DSBs. RECQL4 also directly interacts with CtIP via its N-terminal domain and promotes CtIP recruitment to the MRN complex at DSBs. Moreover, inactivation of RECQL4's helicase activity impairs DNA end processing and HR-dependent DSBR without affecting its interaction with MRE11 and CtIP, suggesting an important role for RECQL4's unwinding activity in the process. Thus, we report that RECQL4 is an important participant in HR-dependent DSBR.

Keywords: DNA repair; DNA resection; RECQL4; RecQ-like helicase; Rothmund-Thomson syndrome; homologous recombination.

MeSH terms

  • Carrier Proteins
  • Cell Line, Tumor
  • DNA Breaks, Double-Stranded*
  • DNA End-Joining Repair*
  • DNA Repair Enzymes / metabolism
  • Exodeoxyribonucleases / metabolism
  • Humans
  • MRE11 Homologue Protein / metabolism
  • Nuclear Proteins
  • RecQ Helicases / metabolism*
  • Recombinational DNA Repair
  • Replication Protein A / metabolism
  • Repressor Proteins

Substances

  • BCL11A protein, human
  • Carrier Proteins
  • MRE11 protein, human
  • Nuclear Proteins
  • Replication Protein A
  • Repressor Proteins
  • EXO1 protein, human
  • Exodeoxyribonucleases
  • MRE11 Homologue Protein
  • Bloom syndrome protein
  • RECQL4 protein, human
  • RecQ Helicases
  • DNA Repair Enzymes