Nucleic Acids Research Advance Access published online on September 29, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl604
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© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
1 Abteilung Molekulare Genetik und Präparative Molekularbiologie, Institut für Mikrobiologie und Genetik Georg-August-Universität Göttingen, Grisebachstrasse 8, 37077 Göttingen, Germany 2 Department of Biology (Area 5), University of York PO Box 373, York, YO10 5YW, UK 3 Bioanalytical Mass Spectrometry Group, Max-Planck Institute for Biophysical Chemistry Am Fassberg 11, 37077 Göttingen, Germany 4 Ruhr-Universität Bochum, Fakultät Chemie AG Bioorganische Chemie, Universitätsstrasse 150, 44780 Bochum, Germany
*To whom correspondence should be addressed. Tel: +49 551 39 3804; Fax: +49 551 39 3805; Email: hfritz1{at}gwdg.de
Received May 9, 2006. Revised July 13, 2006. Accepted August 3, 2006.
The genome of Methanothermobacter thermautotrophicus, as a hitherto unique case, is apparently devoid of genes coding for general uracil DNA glycosylases, the universal mediators of base excision repair following hydrolytic deamination of DNA cytosine residues. We have now identified protein Mth212, a member of the ExoIII family of nucleases, as a possible initiator of DNA uracil repair in this organism. This enzyme, in addition to bearing all the enzymological hallmarks of an ExoIII homologue, is a DNA uridine endonuclease (U-endo) that nicks double-stranded DNA at the 5'-side of a 2'-d-uridine residue, irrespective of the nature of the opposing nucleotide. This type of activity has not been described before; it is absent from the ExoIII homologues of Escherichia coli, Homo sapiens and Methanosarcina mazei, all of which are equipped with uracil DNA repair glycosylases. The U-endo activity of Mth212 is served by the same catalytic center as its AP-endo activity.
Present address: Jens Georg, Institute of Biology II/Experimental Bioinformatics, University of Freiburg, Schänzlestrasse 1, D-79104 Freiburg, Germany
Present address: Alan I. Majerník, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Moyzesova 61, 900 28 Ivanka pri Dunaji, Slovak Republic
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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