Tn7 transposition: Target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system

Roland J. Bainton, Kenneth M. Kubo, Jian nong Feng, Nancy L. Craig

Research output: Contribution to journalArticle

Abstract

We have reconstituted the transposition of the bacterial transposon TO into its specific insertion site attTn7 with four purified Tn7-encoded proteins, TnsA+TnsB+ TnsC+TnsD, and ATP. TnsA+TnsB+TnsC form a "core" recombination machine that recognizes the transposon ends and executes DNA breakage and joining; TnsD specifically recognizes attTn7. TnsA+TnsB+TnsC are specifically targeted to attTn7 through the TnsD-dependent interaction of TnsC, a nonspecific DNA-binding protein, with attTn7. Recombination appears to be activated by the assembly of a nucleoprotein complex containing the DNA substrates and Tns proteins. We suggest that TnsC plays a central role in communication between the transposon and the target DNA, particularly in directing insertion away from DNAs already containing a copy of Tn7.

Original languageEnglish (US)
Pages (from-to)931-943
Number of pages13
JournalCell
Volume72
Issue number6
DOIs
StatePublished - Mar 26 1993

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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