Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11

Matthew D. Nichols, Kristen DeAngelis, James L. Keck, James M. Berger

Research output: Contribution to journalArticlepeer-review

Abstract

In all organisms, type II DNA topoisomerases are essential for untangling chromosomal DNA. We have determined the structure of the DNA-binding core of the Methanococcus jannaschii DNA topoisomerase VIA subunit at 2.0 Å resolution. The overall structure of this subunit is unique, demonstrating that archaeal type II enzymes are distinct from other type II topoisomerases. However, the core structure contains a pair of domains that are also found in type IA and classic type II topoisomerases. Together, these regions may form the basis of a DNA cleavage mechanism shared among these enzymes. The core A subunit is a dimer that contains a deep groove that spans both protomers. The dimer architecture suggests that DNA is bound in the groove, across the A subunit interface, and that the two monomers separate during DNA transport. The A subunit of topoisomerase VI is homologous to the meiotic recombination factor, Spo11, and this structure can serve as a template for probing Spo11 function in eukaryotes.

Original languageEnglish (US)
Pages (from-to)6177-6188
Number of pages12
JournalEMBO Journal
Volume18
Issue number21
DOIs
StatePublished - Nov 1 1999
Externally publishedYes

Keywords

  • DNA-binding protein
  • Spo11
  • Topoisomerase

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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