Use of suppressor analysis to identify DNA polymerase mutations in herpes simplex virus which affect deoxynucleoside triphosphate substrate specificity.
作者信息
Wang Y S, Woodward S, Hall J D
机构信息
Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721.
出版信息
J Virol. 1992 Mar;66(3):1814-6. doi: 10.1128/JVI.66.3.1814-1816.1992.
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.
摘要
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