Structural and functional relationships of the XPF/MUS81 family of proteins.

Abstract

Proteins belonging to the XPF/MUS81 family play important roles in the repair of DNA lesions caused by UV-light or DNA cross-linking agents. Most eukaryotes have four family members that assemble into two distinct heterodimeric complexes, XPF-ERCC1 and MUS81-EME1. Each complex contains one catalytic and one noncatalytic subunit and exhibits endonuclease activity with a variety of 3'-flap or fork DNA structures. The catalytic subunits share a characteristic core containing an excision repair cross complementation group 4 (ERCC4) nuclease domain and a tandem helix-hairpin-helix (HhH)(2) domain. Diverged domains are present in the noncatalytic subunits and may be required for substrate targeting. Vertebrates possess two additional family members, FANCM and Fanconi anemia-associated protein 24 kDa (FAAP24), which possess inactive nuclease domains. Instead, FANCM contains a functional Superfamily 2 (SF2) helicase domain that is required for DNA translocation. Determining how these enzymes recognize specific DNA substrates and promote key repair reactions is an important challenge for the future.

DOI: 10.1146/annurev.biochem.77.070306.102408
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@article{Ciccia2008StructuralAF, title={Structural and functional relationships of the XPF/MUS81 family of proteins.}, author={Alberto Ciccia and Neil E McDonald and Stephen C West}, journal={Annual review of biochemistry}, year={2008}, volume={77}, pages={259-87} }