Nucleic Acids Research, Vol 25, Issue 20 4061-4066, Copyright © 1997 by Oxford University Press
C Rudy, KL Taylor, D Hinerfeld, JR Scott and G Churchward
The roles of purified Int and Xis proteins of the conjugative transposon Tn
916 in excision of a deletion derivative of the closely related element Tn
1545 were investigated. At a low salt concentration (37.5 mM NaCl), Int
alone was able to promote limited excision to produce a covalently closed
circular form of the transposon, showing that Tn 916 Int can catalyze both
DNA cleavage and strand exchange. This reaction was stimulated by Xis. At
higher salt concentrations (150 mM NaCl), excision by Int alone was reduced
to barely detectable levels and Xis was required for excision. The low
salt, Xis-stimulated reaction was approximately 8-fold more efficient than
the high salt, Xis-dependent reaction. These results reflect in vivo
requirements for Int and Xis in excision.
ARTICLES
Excision of a conjugative transposon in vitro by the Int and Xis proteins of Tn916
Department of Microbiology and Immunology, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA.
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