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Nucleic Acids Research, 1992, Vol. 20, No. 22 6075-6080
© 1992

ENZYMOLOGY

DNA substrate specificity of DNA helicase E from calf thymus

John J. Turchi1, Richard S. Murante and Robert A. Bambara1,*

Department of Biochemistry Rochester, NY 14642, USA 1Cancer Center, University of Rochester School of Medicine and Dentistry Rochester, NY 14642, USA

* To whom correspondence should be addressed at: Department of Biochemistry, University of Rochester Medical Center, Box 607, 601 Elmwood Avenue, Rochester, NY 14642, USA

Received June 4, 1992. Revised October 20, 1992. Accepted October 20, 1992.

DNA helicase E from calf thymus has been characterized with respect to DNA substrate specificity. The helicase was capable of displacing DNA fragments up to 140 nucleotides in length, but was unable to displace a DNA fragment 322 nucleotides in length. DNA competition experiments revealed that helicase E was moderately processive for translocation on single strand M13mp18 DNA, and that the helicase would dissociate and rebind during a 15 minute reaction. Comparison of the rate of ATPase activity catalyzed by helicase E on single strand DNA substrates of different lengths, suggested a processivity consistent with the competition experiments. The helicase displayed a preference for displacing primers whose 5' terminus was fully annealed as opposed to primers with a 12 nucleotide 5' unannealed tail. The presence of a 12 nucleotide 3' tail had no effect on the rate of displacement. DNA helicase E was capable of displacing a primer downstream of either a four nucleotide gap, a one nucleotide gap or a nick in the DNA substrate. Helicase E was inactive on a fully duplex DNA 30 base pairs in length. Calf thymus RP-A stimulated the DNA displacement activity of helicase E. These properties are consistent with a role for DNA helicase E in chromosomal DNA repair.


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