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Characterization of a Nudix hydrolase from <Emphasis Type="Italic">Deinococcus radiodurans</Emphasis> with a marked specificity for (deoxy)ribonucleoside 5'-diphosphates |
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| Authors: | David?I?Fisher Jared?L?Cartwright Hideyoshi?Harashima Hiroyuki?Kamiya |
| Institution: | (1) School of Biological Sciences, Biosciences Building, University of Liverpool, P.O. Box 147, Liverpool, L69 7ZB, UK;(2) Department of Biology, University of York, P.O. Box 373, York, YO10 5YW, UK;(3) Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo 060-0812, Japan |
| Abstract: | BackgroundNudix hydrolases form a protein family whose function is to hydrolyse intracellular nucleotides and so regulate their levels and eliminate potentially toxic derivatives. The genome of the radioresistant bacterium Deinococcus radiodurans encodes 25 nudix hydrolases, an unexpectedly large number. These may contribute to radioresistance by removing mutagenic oxidised and otherwise damaged nucleotides. Characterisation of these hydrolases is necessary to understand the reason for their presence. Here, we report the cloning and characterisation of the DR0975 gene product, a nudix hydrolase that appears to be unique to this organism. |
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