The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease

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,...

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Main Authors:	Georg, Jens, Schomacher, Lars, Chong, James P. J., Majerník, Alan I., Raabe, Monika, Urlaub, Henning, Müller, Sabine, Ciirdaeva, Elena, Kramer, Wilfried, Fritz, Hans-Joachim
Format:	Online
Language:	English
Published:	Oxford University Press 2006
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1636421/

id	pubmed-1636421
recordtype	oai_dc
spelling	pubmed-16364212006-11-29 The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease Georg, Jens Schomacher, Lars Chong, James P. J. Majerník, Alan I. Raabe, Monika Urlaub, Henning Müller, Sabine Ciirdaeva, Elena Kramer, Wilfried Fritz, Hans-Joachim Nucleic Acid Enzymes 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. Oxford University Press 2006-10 2006-09-29 /pmc/articles/PMC1636421/ /pubmed/17012282 http://dx.doi.org/10.1093/nar/gkl604 Text en © 2006 The Author(s)
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Georg, Jens Schomacher, Lars Chong, James P. J. Majerník, Alan I. Raabe, Monika Urlaub, Henning Müller, Sabine Ciirdaeva, Elena Kramer, Wilfried Fritz, Hans-Joachim
spellingShingle	Georg, Jens Schomacher, Lars Chong, James P. J. Majerník, Alan I. Raabe, Monika Urlaub, Henning Müller, Sabine Ciirdaeva, Elena Kramer, Wilfried Fritz, Hans-Joachim The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
author_facet	Georg, Jens Schomacher, Lars Chong, James P. J. Majerník, Alan I. Raabe, Monika Urlaub, Henning Müller, Sabine Ciirdaeva, Elena Kramer, Wilfried Fritz, Hans-Joachim
author_sort	Georg, Jens
title	The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
title_short	The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
title_full	The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
title_fullStr	The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
title_full_unstemmed	The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease
title_sort	methanothermobacter thermautotrophicus exoiii homologue mth212 is a dna uridine endonuclease
description	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.
publisher	Oxford University Press
publishDate	2006
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1636421/
_version_	1611390669719339008

The Methanothermobacter thermautotrophicus ExoIII homologue Mth212 is a DNA uridine endonuclease

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