Homology between DNA polymerases of poxviruses, herpesviruses, and adenoviruses: nucleotide sequence of the vaccinia virus DNA polymerase gene.

Abstract

A 5400-base-pair segment of the vaccinia virus genome was sequenced and an open reading frame of 938 codons was found precisely where the DNA polymerase had been mapped by transfer of a phosphonoacetate-resistance marker. A single nucleotide substitution changing glycine at position 347 to aspartic acid accounts for the drug resistance of the mutant vaccinia virus. The 5' end of the DNA polymerase mRNA was located 80 base pairs before the methionine codon initiating the open reading frame. Correspondence between the predicted Mr 108,577 polypeptide and the 110,000 purified enzyme indicates that little or no proteolytic processing occurs. Extensive homology, extending over 435 amino acids, was found upon comparing the DNA polymerase of vaccinia virus and DNA polymerase of Epstein-Barr virus. A highly conserved sequence of 14 amino acids in the carboxyl-terminal regions of the above DNA polymerases is also present at a similar location in adenovirus DNA polymerase. This structure, which is predicted to form a turn flanked by (3-pleated sheets, may form part of an essential binding or catalytic site that accounts for its presence in DNA polymerases of poxviruses, herpesviruses, and adenoviruses.

Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat

“…After the construction of restriction maps (Wittek et al, 1977;Mackett & Archard, 1979) and the cloning of individual restriction fragments (Wittek et al, 1980;Belle Isle et al, 1981), the 186kb genome of the laboratory strain of vaccinia virus (Western Reserve, WR) has been studied in detail. The structure of the terminal hairpins has been determined and the complete sequence of several of the viral HindIII restriction fragments and many individual genes have been reported from WR and other strains of virus (Ahn et al, 1990;Amegadzie et al, 1991;Baldick & Moss, 1987;Boursnell et al, 1988;Bertholet et al,, 1985;Broyles & Moss, 1986;Earl et al, 1986;Gillard et al, 1986;Gordon et al, 1988;Hirt et al, 1986;Howard & Smith, 1989;Howard et al, 1991 ;Jin et al, 1989;Kotwal & Moss, 1988aNiles et al, 1986;Plucienniczak et al, 1985;Rodriguez et al, 1986;Rodriguez & Esteban, 1987;Rosel et al, 1986;Rosel & Moss, 1985;Roseman & Hruby, 1987;Roseman & Slabaugh, 1990;Schmitt & Stunnenberg, 1989;Slabaugh & Roseman, 1989;Slabaugh et al, 1988;Shida, 1986;Smith et al, 1989a, b, c;Smith & Chan, 1991;Tamin et al, 1988;Tengelsen et al, 1988;Traktman et al, 1989;Tsoa et al, 1986;…”

Cloning and Characterization of the Gene Encoding the Major Protein of the A-type Inclusion Body of Cowpox Virus

“…Structural and functional analyses of viral polypeptides synthesized in infected cells have revealed at least two late gene subsets that can be defined temporally (Pennington, 1974;Ichihashi et aL, 1971). The fine structures of several early and late VV genes have been determined (Bertholet et al, 1985(Bertholet et al, , 1986Cochran et al, 1985;Plucienniczak et al, 1985 ;H~inggi et al, 1986;Rosel et al, 1986;Weir & Moss, 1987;Weinrich & Hruby, 1986;Niles et al, 1986;Earl et al, 1986), and comparison of nucleotide sequences upstream from these genes has revealed that VV promoters lack both eukaryotic and prokaryotic consensus sequences. Instead they have characteristic signals (Venkatesan et al, 1981(Venkatesan et al, , 1982Weir & Moss, 1983) recognized by VV RNA polymerase but not by the cellular RNA polymerase II (Puckett & Moss, 1983).…”

Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins

“…When the predicted amino acid sequences of all VV genes present in the data banks were searched for the presence of an Ala-Gly-Ala motif, three occurrences were noted: the 32.5K host-range factor (Gillard et al, 1986), the DNA polymerase gene (Earl et al, 1986) and the palmitated 37K protein associated with extracellular enveloped virions (Hiller & Weber, 1985;Hirt et al, 1986). To date, none of these three proteins has been reported to undergo proteolytic processing during infection.…”