X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: Similarity between its endonuclease domain and restriction enzymes

Tatsuya Nishino, Kayoko Komori, Yoshizumi Ishino, Kosuke Morikawa

研究成果: Contribution to journalArticle

88 引用 (Scopus)

抜粋

The XPF/Rad1/Mus81-dependent nuclease family specifically cleaves branched structures generated during DNA repair, replication, and recombination, and is essential for maintaining genome stability. Here, we report the domain organization of an archaeal homolog (Hef) of this family and the X-ray crystal structure of the middle domain, with the nuclease activity. The nuclease domain architecture exhibits remarkable similarity to those of restriction endonucleases, including the correspondence of the GDXnERKX3D signature motif in Hef to the PDXn(E/D)XK motif in restriction enzymes. This structural study also suggests that the XPF/Rad1/Mus81/ERCC1 proteins form a dimer through each interface of the nuclease domain and the helix-hairpin-helix domain. Simultaneous disruptions of both interfaces result in their dissociation into separate monomers, with strikingly reduced endonuclease activities.

元の言語英語
ページ(範囲)445-457
ページ数13
ジャーナルStructure
11
発行部数4
DOI
出版物ステータス出版済み - 4 1 2003

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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