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Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition.

Newman M, Murray-Rust J, Lally J, Rudolf J, Fadden A, Knowles PP, White MF, McDonald NQ
EMBO J 24 895-905 (2005)
Cited: 78 times
EuropePMC logo PMID: 15719018

Abstract

The XPF/Mus81 structure-specific endonucleases cleave double-stranded DNA (dsDNA) within asymmetric branched DNA substrates and play an essential role in nucleotide excision repair, recombination and genome integrity. We report the structure of an archaeal XPF homodimer alone and bound to dsDNA. Superposition of these structures reveals a large domain movement upon binding DNA, indicating how the (HhH)(2) domain and the nuclease domain are coupled to allow the recognition of double-stranded/single-stranded DNA junctions. We identify two nonequivalent DNA-binding sites and propose a model in which XPF distorts the 3' flap substrate in order to engage both binding sites and promote strand cleavage. The model rationalises published biochemical data and implies a novel role for the ERCC1 subunit of eukaryotic XPF complexes.

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  1. DNA repair gets physical: mapping an XPA-binding site on ERCC1. Croteau DL, Peng Y, Van Houten B. DNA Repair (Amst) 7 819-826 (2008)

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  4. Current status of excision repair cross complementing-group 1 (ERCC1) in cancer. Gossage L, Madhusudan S. Cancer Treat Rev 33 565-577 (2007)
  5. DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy. McNeil EM, Melton DW. Nucleic Acids Res 40 9990-10004 (2012)
  6. Regulation of endonuclease activity in human nucleotide excision repair. Fagbemi AF, Orelli B, Schärer OD. DNA Repair (Amst) 10 722-729 (2011)
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  11. Function and Interactions of ERCC1-XPF in DNA Damage Response. Faridounnia M, Folkers GE, Boelens R. Molecules 23 E3205 (2018)
  12. DNA repair in hyperthermophilic and hyperradioresistant microorganisms. Ishino Y, Narumi I. Curr Opin Microbiol 25 103-112 (2015)
  13. Overview of xeroderma pigmentosum proteins architecture, mutations and post-translational modifications. Feltes BC, Bonatto D. Mutat Res Rev Mutat Res 763 306-320 (2015)
  14. Structure-Specific Endonucleases and the Resolution of Chromosome Underreplication. Falquet B, Rass U. Genes (Basel) 10 E232 (2019)
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  16. Alkyltransferase-like proteins: molecular switches between DNA repair pathways. Tubbs JL, Tainer JA. Cell Mol Life Sci 67 3749-3762 (2010)
  17. FAN1, a DNA Repair Nuclease, as a Modifier of Repeat Expansion Disorders. Deshmukh AL, Porro A, Mohiuddin M, Lanni S, Panigrahi GB, Caron MC, Masson JY, Sartori AA, Pearson CE. J Huntingtons Dis 10 95-122 (2021)
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