Crystal Structures of the structure-selective nuclease Mus81-Eme1 bound to flap DNA substrates
SCIE
SCOPUS
- Title
- Crystal Structures of the structure-selective nuclease Mus81-Eme1 bound to flap DNA substrates
- Authors
- Gwon, GH; Jo, A; Baek, K; Jin, KS; Fu, Y; Lee, JB; Kim, Y; Cho, Y
- Date Issued
- 2014-05-02
- Publisher
- Nature Publishing Group
- Abstract
- The Mus81-Eme1 complex is a structure-selective endonuclease with a critical role in the resolution of recombination intermediates during DNA repair after interstrand cross-links, replication fork collapse, or double-strand breaks. To explain the molecular basis of 3 ' flap substrate recognition and cleavage mechanism by Mus81-Eme1, we determined crystal structures of human Mus81-Eme1 bound to various flap DNA substrates. Mus81-Eme1 undergoes gross substrate-induced conformational changes that reveal two key features: (i) a hydrophobic wedge of Mus81 that separates pre- and post-nick duplex DNA and (ii) a 5 ' end binding pocket that hosts the 5 ' nicked end of post-nick DNA. These features are crucial for comprehensive protein-DNA interaction, sharp bending of the 3 ' flap DNA substrate, and incision strand placement at the active site. While Mus81-Eme1 unexpectedly shares several common features with members of the 5 ' flap nuclease family, the combined structural, biochemical, and biophysical analyses explain why Mus81-Eme1 preferentially cleaves 3 ' flap DNA substrates with 5 ' nicked ends.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/13700
- DOI
- 10.1002/EMBJ.201487820
- ISSN
- 0261-4189
- Article Type
- Article
- Citation
- EMBO Journal, vol. 33, no. 9, page. 1061 - 1072, 2014-05-02
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