Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli

Hyung Chung Ji, Hyun Young Park, Ho Lee Jong, Yangsoo Jang

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

A hypothetical 21.0 kDa protein (ORF O197) from Escherichia coli K-12 was cloned, purified, and characterized. The protein sequence of ORF O197 (termed EcO197) shares a 33.5% identity with that of a novel NTPase from Methanococcus jannaschii. The EcO197 protein was purified using Ni-NTA affinity chromatography, protease digestion, and gel filtration column. It hydrolyzed nucleoside triphosphates with an O6 atom-containing purine base to nucleoside monophosphate and pyrophosphate. The EcO197 protein had a strong preference for deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP), while it had little activity in the standard nucleoside triphosphates (dATP, dCTP, dGTP, and dTTP). These aberrant nucleotides can be produced by oxidative deamination from purine nucleotides in cells; they are potentially mutagenic. The mutation protection mechanisms are caused by the incorporation into DNA of unwelcome nucleotides that are formed spontaneously. The EcO197 protein may function to eliminate specifically damaged purine nucleotide that contains the 6-keto group. This protein appears to be the first eubacterial dITP- and XTP-hydrolyzing enzyme that has been identified.

Original languageEnglish
Pages (from-to)403-408
Number of pages6
JournalJournal of Biochemistry and Molecular Biology
Volume35
Issue number4
Publication statusPublished - 2002 Jul 1

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Escherichia coli Proteins
Nucleosides
Purine Nucleotides
Proteins
Open Reading Frames
Nucleotides
Nucleoside-Triphosphatase
Methanocaldococcus
Affinity chromatography
Deamination
Affinity Chromatography
Escherichia coli
Gel Chromatography
xanthosine 5'-triphosphate
deoxyinosine
triphosphoric acid
Digestion
Peptide Hydrolases
Gels
Atoms

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

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abstract = "A hypothetical 21.0 kDa protein (ORF O197) from Escherichia coli K-12 was cloned, purified, and characterized. The protein sequence of ORF O197 (termed EcO197) shares a 33.5{\%} identity with that of a novel NTPase from Methanococcus jannaschii. The EcO197 protein was purified using Ni-NTA affinity chromatography, protease digestion, and gel filtration column. It hydrolyzed nucleoside triphosphates with an O6 atom-containing purine base to nucleoside monophosphate and pyrophosphate. The EcO197 protein had a strong preference for deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP), while it had little activity in the standard nucleoside triphosphates (dATP, dCTP, dGTP, and dTTP). These aberrant nucleotides can be produced by oxidative deamination from purine nucleotides in cells; they are potentially mutagenic. The mutation protection mechanisms are caused by the incorporation into DNA of unwelcome nucleotides that are formed spontaneously. The EcO197 protein may function to eliminate specifically damaged purine nucleotide that contains the 6-keto group. This protein appears to be the first eubacterial dITP- and XTP-hydrolyzing enzyme that has been identified.",
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Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli. / Ji, Hyung Chung; Park, Hyun Young; Jong, Ho Lee; Jang, Yangsoo.

In: Journal of Biochemistry and Molecular Biology, Vol. 35, No. 4, 01.07.2002, p. 403-408.

Research output: Contribution to journalArticle

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