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J Biol Chem, Vol. 273, Issue 11, 6024-6029, March 13, 1998
From the Max Planck Institute for Biochemistry, Am Klopferspitz
18a, 82152 Martinsried, Federal Republic of Germany
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.
Biochemical and Phylogenetic Characterization of the dUTPase from
the Archaeal Virus SIRV
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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