The vaccinia virus D5 protein, which is required for DNA replication, is a nucleic acid-independent nucleoside triphosphatase. J Virol 1995 Sep;69(9):5353-61
Date
09/01/1995Pubmed ID
7636979Pubmed Central ID
PMC189376DOI
10.1128/JVI.69.9.5353-5361.1995Scopus ID
2-s2.0-0029149630 (requires institutional sign-in at Scopus site) 67 CitationsAbstract
The vaccinia virus D5 gene encodes a 90-kDa protein that is transiently expressed at early times after infection. Temperature-sensitive mutants with lesions in the D5 gene exhibit a fast-stop DNA- phenotype and are also impaired in homologous recombination. Here we report the overexpression of the D5 protein within the context of a vaccinia virus infection and its purification to apparent homogeneity. The purified protein has an intrinsic nucleoside triphosphatase activity which is independent of, and not stimulated by, any common nucleic acid cofactors. All eight common ribo- and deoxyribonucleoside triphosphates are hydrolyzed to the diphosphate form in the presence of a divalent cation. Implications for the role of D5 in viral DNA replication are addressed.
Author List
Evans E, Klemperer N, Ghosh R, Traktman PMESH terms used to index this publication - Major topics in bold
Acid Anhydride HydrolasesAdenosine Triphosphatases
Cell Line
Chromatography, Affinity
Chromatography, DEAE-Cellulose
DNA Replication
Genes, Viral
Humans
Kinetics
Mutagenesis
Nucleoside-Triphosphatase
Recombinant Proteins
Restriction Mapping
Temperature
Transfection
Vaccinia virus
Viral Proteins
