Biochemical Characterization of TT1383 from Thermus thermophilus Identifies a Novel dNTP Triphosphohydrolase Activity Stimulated by dATP and dTTP

Authors: Naoyuki Kondo; Seiki Kuramitsu; Ryoji Masui

Source: The Journal of Biochemistry, Volume 136, Number 2, August 2004 , pp. 221-231(11)

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Abstract:

The HD domain motif is found in a superfamily of proteins in bacteria, archaea and eukaryotes. A few of these proteins are known to have metal-dependant phosphohydrolase activity, but the others are functionally unknown. Here we have characterized an HD domain-containing protein, TT1383, from Thermus thermophilus HB8. This protein has sequence similarity to Escherichia coli dGTP triphosphohydrolase, however, no dGTP hydrolytic activity was detected. The hydrolytic activity of the protein was determined in the presence of more than two kinds of deoxyribonucleoside triphosphates (dNTPs), which were hydrolyzed to their respective deoxyribonucleosides and triphosphates, and was found to be strictly specific for dNTPs in the following order of relative activity: dCTP > dGTP > dTTP > dATP. Interestingly, this dNTP triphosphohydrolase (dNTPase) activity requires the presence of dATP or dTTP in the dNTP mixture. dADP, dTDP, dAMP, and dTMP, which themselves were not hydrolyzed, were nonetheless able to stimulate the hydrolysis of dCTP. These results suggest the existence of binding sites specific for dATP and dTTP as positive modulators, distinct from the dNTPase catalytic site. This is, to our knowledge, the first report of a non-specific dNTPase that is activated by dNTP itself.

Document Type: Research article

DOI: http://dx.doi.org/10.1093/jb/mvh115

Affiliations: 1: Department of Biology, Graduate School of Science, Osaka University, Toyonaka 560-0043; and

Publication date: 2004-08-01