| http://purl.uniprot.org/citations/3012520 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3012520 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3012520 | http://www.w3.org/2000/01/rdf-schema#comment | "Herpesvirus saimiri (HVS) is the prototype member of a distinctive subset of lymphotropic herpesviruses (the gamma 2 subgroup) with A+T-rich coding sequences. In this paper, we show that cells productively infected with HVS contain high concentrations of a virus-specified thymidylate synthase (5,10-methylenetetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45); we identify the active polypeptide and present the sequence of the virus gene. The predicted amino acid sequence of the 294-residue subunit of the virus enzyme is 70% homologous with the sequence of the human enzyme and about 50% homologous with prokaryotic thymidylate synthases, illustrating the remarkable structural constraints imposed by the thymidylate synthase function. However, the presence of the enzyme is not a conserved property of herpesviruses. We find no evidence for a virus-encoded thymidylate synthase activity (or a homology to a thymidylate synthase sequence) in G+C-rich representatives of alpha 1 (e.g., herpes simplex viruses, 66-68% G+C), beta (i.e., human cytomegalovirus, 58-59% G+C), and gamma 1 (i.e., Epstein-Barr virus, 60% G+C) herpesvirus subgroups. The production of excess thymidylate by a virus thymidylate synthase in cells infected with an A+T-rich herpesvirus would provide one plausible source of biased mutations by the virus-encoded replicative enzymes, which we have previously suggested as the likely general cause of differences in the mean nucleotide compositions of herpesvirus genomes."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.83.11.3604"xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.83.11.3604"xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Cameron K.R."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Cameron K.R."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Fleckenstein B."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Fleckenstein B."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Honess R.W."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Honess R.W."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Niller H.H."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Niller H.H."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Randall R.E."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Randall R.E."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Bodemer W."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/author | "Bodemer W."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/pages | "3604-3608"xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/pages | "3604-3608"xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/title | "The A+T-rich genome of Herpesvirus saimiri contains a highly conserved gene for thymidylate synthase."xsd:string |
| http://purl.uniprot.org/citations/3012520 | http://purl.uniprot.org/core/title | "The A+T-rich genome of Herpesvirus saimiri contains a highly conserved gene for thymidylate synthase."xsd:string |