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Use of suppressor analysis to identify DNA polymerase mutations in herpes simplex virus which affect deoxynucleoside
Y S Wang1, S Woodward, J D Hall
1Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721.
Journal of Virology
|March 1, 1992
Abstract:
Herpes simplex virus DNA polymerase mutations which map in the N-terminal part of the protein and appear to alter deoxynucleoside triphosphate (dNTP) substrate specificity are described. These mutations suppress a drug hypersensitivity associated with the downstream mutation, Aphr10. We suggest that the mutant residues form part of the dNTP-binding site, a site previously thought to be confined to the C terminus.