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Nucleic Acids Research, 1988, Vol. 16, No. 7 2765-2785
© 1988

Articles

Terminase host factor: a histone-like E.coli protein which can bind to the cos region of bacteriophage {lambda} DNA

Gayle Shinder, Wendy Parris and Marvin Gold*

Department of Medical Genetics, University of Toronto Toronto M5S 1A8, Canada

*To whom corresponence should be addressed

Received November 11, 1987. Revised February 16, 1988. Accepted February 16, 1988.

Terminase Host Factor (THF), an E. coli protein capable of fulfilling the host factor requirement for in vitro bacteriophage {lambda} terminase activity, displays properties characteristic of the prokaryotic type II DNA-binding or "histone-like" proteins. It is a 22 K basic, heat- and acid-stable protein which binds non-specifically to various DNAs. Conditions can be established, however, where THF binds preferentially to the cohesive end site (cos) of {lambda}DNA forming several distinct complexes as visualized by band retardation in polyacrylamide gels. DNase I footprinting reveals that THF can protect several regions of the top (l) strand on the right side (+) of cos but does not bind as well to the left side (–). The binding regions are separated either by unprotected or by DNase I-hypersensitive bases. Under the conditions used in these experiments, DNA which does not contain cos {lambda} sequences does not show this pattern of protection. Several repeated motifs in the cos {lambda} nucleotide sequence may represent a consensus sequence for THF interaction. THF may be similar to other "histone-like" proteins which display both non-specific and selective DNA-binding capacities.


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