Nucleic Acids Research, 1989, Vol. 17, No. 1 317-334
© 1989
MOLECULAR BIOLOGY |
The interaction of E.coli integration host factor and 
cos DNA: multiple complex formation and protein-induced bending
Department of Molecular Biology and Biochemistry, Hall-Atwater Laboratory, Wesleyan University Middletown, CT 06457, USA 1Department of Medical Genetics, Medical Sciences Building, University of Toronto Toronto, Ontario M5S 1A8, Canada
The Interaction of E. colis Integration Host Factor (IHF) with fragments of lambda DNA containing the cos site has been studied by gel-mobllity retardation and electron microscopy. The cos fragment used in the mobility assays Is 398 bp and spans a region from 48, 298 to 194 on the lambda chromosome. Several different complexes of IHF with this fragment can be distinguished by their differential mobllity on polyacrylamide gels. Relative band intensities indicate that the formation of a complex between IHF and this DNA fragment has an equilibrium binding constant of the same magnitude as DNA fragments containing lambda's attP site. Gel-mobility retardation and electron microscopy have been employed to show that IHF sharply bends DNA near cos and to map the bending site. The protein-induced bend is near an intrinsic bend due to DNA sequence. The position of the bend suggests that IHF's rote in lambda DNA packaging may be the enhancement of terminase binding/cos cutting by manipulating DNA structure.
+Present address: Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario NIG 2W1, Canada
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