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

Research output: Contribution to journalArticle

88 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)445-457
Number of pages13
JournalStructure
Volume11
Issue number4
DOIs
Publication statusPublished - Apr 1 2003

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Genomic Instability
Endonucleases
DNA Restriction Enzymes
DNA Replication
DNA Repair
Genetic Recombination
Anatomy
X-Rays
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease : Similarity between its endonuclease domain and restriction enzymes. / Nishino, Tatsuya; Komori, Kayoko; Ishino, Yoshizumi; Morikawa, Kosuke.

In: Structure, Vol. 11, No. 4, 01.04.2003, p. 445-457.

Research output: Contribution to journalArticle

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