Unexpected structural diversity in DNA recombination: The restriction endonuclease connection

Alison Burgess Hickman, Ying Li, Shiny Varghese Mathew, Earl W. May, Nancy L. Craig, Fred Dyda

Research output: Contribution to journalArticlepeer-review

94 Scopus citations


Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 Å resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.

Original languageEnglish (US)
Pages (from-to)1025-1034
Number of pages10
JournalMolecular cell
Issue number6
StatePublished - 2000

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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