Journal
DNA REPAIR
Volume 4, Issue 1, Pages 33-39Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.dnarep.2004.07.010
Keywords
Orf17 (NtpA); MutT; 8-hydroxy-dATP; 8-hydroxy-dADP; nucleotide pool sanitization
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To determine whether the Orf17 (NtpA) protein of Escherichia coli, a MutT-type enzyme, functions as a hydrolyzing enzyme for a damaged deoxyribonucleotide, we purified the recombinant Orf17 protein and incubated it with oxidized deoxyribonucleotides. Of the deoxyribonucleoside 5'-triphosphates tested, 8-hydroxy-2'-deoxyadenosine 5'-triphosphate was hydrolyzed by this protein. Unexpectedly, the Orf17 protein degraded 8-hydroxy-2'-deoxyadenosine 5-diphosphate 2.3-fold more efficiently than the corresponding triphosphate. Thus, this protein is the first MutT-type enzyme that hydrolyzes both the triphosphate and diphosphate derivatives of a deoxyribonucleoside, with similar efficiencies. These results suggest that the Orf17 protein may be involved in the hydrolysis of oxidized dATP and dADP. (C) 2004 Elsevier B.V. All rights reserved.
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