ATP-dependent specific binding of Tn3 transposase to Tn3 inverted repeats

W. L. Wishart, J. R. Broach, E. Ohtsubo

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Transposons are discrete segments of DNA which are capable of moving from one site in a genome to many different sites1,2. Tn3 is a prokaryotic transposon which is 4,957 base pairs (bp) long and encodes a transposase protein which is essential for transposition3-7. We report here a simple method for purifying Tn3 transposase and demonstrate that the transposase protein binds specifically to the ends of the Tn3 transposon in an ATP-dependent manner. The transposase protein binds to linear double-stranded DNA both nonspecifically and specifically; the nonspecific DNA binding activity is sensitive to challenge with heparin. Site-specific DNA binding to the ends (inverted repeats) of Tn3 is observed only when binding is performed in the presence of ATP; this ATP-dependent site-specific DNA binding activity is resistant to heparin challenge. Our results indicate that ATP qualitatively alters the DNA binding activity of the transposase protein so that the protein is able to bind specifically to the ends of the Tn3 transposon.

Original languageEnglish (US)
Pages (from-to)556-558
Number of pages3
JournalNature
Volume314
Issue number6011
DOIs
StatePublished - Dec 1 1985

All Science Journal Classification (ASJC) codes

  • General

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