Hjc resolvase is a distantly related member of the type II restriction endonuclease family

Hiromi Daiyasu, Kayoko Komori, Shinzi Sakae, Yoshizumi Ishino, Hiroyuki Toh

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

Abstract

Hjc resolvase is an archael enzyme involved in homologous DNA recombination at the Holliday junction intermediate. However, the structure and the catalytic mechanism of the enzyme have not yet been identified. We performed database searching using the amino acid sequence of the enzyme from Pyrococcus furiosus as a query. We detected 59 amino acid sequences showing weak but significant sequence similarity to the Hjc resolvase. The detected sequences included DpnII, HaeII and Vsr endonuclease, which belong to the type II restriction endonuclease family. In addition, a highly conserved region was identified from a multiple alignment of the detected sequences, which was similar to an active site of the type II restriction endonucleases. We substituted three conserved amino acid residues in the highly conserved region of the Hjc resolvase with Ala residues. The amino acid replacements inactivated the enzyme. The experimental study, together with the results of the database searching, suggests that the Hjc resolvase is a distantly related member of the type II restriction endonuclease family. In addition, the results of our database searches suggested that the members of the RecB domain superfamily are evolutionarily related to the type II restriction endonuclease family.

Original languageEnglish
Pages (from-to)4540-4543
Number of pages4
JournalNucleic acids research
Volume28
Issue number22
DOIs
Publication statusPublished - Nov 15 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics

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