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A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability.

Molecular cell | Mar 26, 2010

FANCM remodels branched DNA structures and plays essential roles in the cellular response to DNA replication stress. Here, we show that FANCM forms a conserved DNA-remodeling complex with a histone-fold heterodimer, MHF. We find that MHF stimulates DNA binding and replication fork remodeling by FANCM. In the cell, FANCM and MHF are rapidly recruited to forks stalled by DNA interstrand crosslinks, and both are required for cellular resistance to such lesions. In vertebrates, FANCM-MHF associates with the Fanconi anemia (FA) core complex, promotes FANCD2 monoubiquitination in response to DNA damage, and suppresses sister-chromatid exchanges. Yeast orthologs of these proteins function together to resist MMS-induced DNA damage and promote gene conversion at blocked replication forks. Thus, FANCM-MHF is an essential DNA-remodeling complex that protects replication forks from yeast to human.

Pubmed ID: 20347428 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Cell Line | Chickens | DNA | DNA Damage | DNA Helicases | DNA Replication | DNA-Binding Proteins | Evolution, Molecular | Genomic Instability | Histones | Humans | Molecular Sequence Data | Protein Binding | Protein Folding | Protein Multimerization | Saccharomyces cerevisiae | Schizosaccharomyces | Sequence Alignment | Sister Chromatid Exchange

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Associated grants

  • Agency: NHLBI NIH HHS, Id: T32 HL007781
  • Agency: Intramural NIH HHS, Id: Z99 AG999999
  • Agency: NIA NIH HHS, Id: Z01 AG000688
  • Agency: NCI NIH HHS, Id: R01 CA112775
  • Agency: Intramural NIH HHS, Id: ZIA AG000688-08
  • Agency: NHLBI NIH HHS, Id: HL007781
  • Agency: Wellcome Trust, Id: CA112775
  • Agency: NCI NIH HHS, Id:

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