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Biochemical and phylogenetic characterization of the dUTPase from the archaeal virus SIRV.
Prangishvili, D; Klenk, H P; Jakobs, G; Schmiechen, A; Hanselmann, C; Holz, I; Zillig, W.
Afiliação
  • Prangishvili D; Max Planck Institute for Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Federal Republic of Germany. Prangish@biochem.mpg.de
J Biol Chem ; 273(11): 6024-9, 1998 Mar 13.
Article em En | MEDLINE | ID: mdl-9497317
ABSTRACT
The derived amino acid sequence from a 474-base pair open reading frame in the genome of the Sulfolobus islandicus rod-shaped virus SIRV shows striking similarity to bacterial dCTP deaminases and to dUTPases from eukaryotes, bacteria, Poxviridae, and Retroviridae. The putative gene was expressed in Escherichia coli, and dUTPase activity of the recombinant enzyme was demonstrated by hydrolysis of dUTP to dUMP. Deamination of dCTP by the enzyme was not detected. Phylogenetic analysis based on amino acid sequences of the characterized enzyme and its homologues showed that the dUTPase-encoding dut genes and the dCTP deaminase-encoding dcd genes constitute a paralogous gene family. This report is the first identification and functional characterization of an archaeal dUTPase and the first phylogeny derived for the dcd-dut gene family.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pirofosfatases / Vírus / Sulfolobus Idioma: En Ano de publicação: 1998 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pirofosfatases / Vírus / Sulfolobus Idioma: En Ano de publicação: 1998 Tipo de documento: Article