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EXOG, a novel paralog of Endonuclease G in higher eukaryotes

Evolutionary conserved mitochondrial nucleases are involved in programmed cell death and normal cell proliferation in lower and higher eukaryotes. The endo/exonuclease Nuc1p, also termed ‘yeast Endonuclease G (EndoG)’, is a member of this class of enzymes that differs from mammalian homologs by the...

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Autores principales: Cymerman, Iwona A., Chung, Inn, Beckmann, Benedikt M., Bujnicki, Janusz M., Meiss, Gregor
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275078/
https://www.ncbi.nlm.nih.gov/pubmed/18187503
http://dx.doi.org/10.1093/nar/gkm1169
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author Cymerman, Iwona A.
Chung, Inn
Beckmann, Benedikt M.
Bujnicki, Janusz M.
Meiss, Gregor
author_facet Cymerman, Iwona A.
Chung, Inn
Beckmann, Benedikt M.
Bujnicki, Janusz M.
Meiss, Gregor
author_sort Cymerman, Iwona A.
collection PubMed
description Evolutionary conserved mitochondrial nucleases are involved in programmed cell death and normal cell proliferation in lower and higher eukaryotes. The endo/exonuclease Nuc1p, also termed ‘yeast Endonuclease G (EndoG)’, is a member of this class of enzymes that differs from mammalian homologs by the presence of a 5′–3′ exonuclease activity in addition to its broad spectrum endonuclease activity. However, this exonuclease activity is thought to be essential for a function of the yeast enzyme in DNA recombination and repair. Here we show that higher eukaryotes in addition to EndoG contain its paralog ‘EXOG’, a novel EndoG-like mitochondrial endo/exonuclease. We find that during metazoan evolution duplication of an ancestral nuclease gene obviously generated the paralogous EndoG- and EXOG-protein subfamilies in higher eukaryotes, thereby maintaining the full endo/exonuclease activity found in mitochondria of lower eukaryotes. We demonstrate that human EXOG is a dimeric mitochondrial enzyme that displays 5′–3′ exonuclease activity and further differs from EndoG in substrate specificity. We hypothesize that in higher eukaryotes the complementary enzymatic activities of EndoG and EXOG probably together account for both, the lethal and vital functions of conserved mitochondrial endo/exonucleases.
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spelling pubmed-22750782008-04-07 EXOG, a novel paralog of Endonuclease G in higher eukaryotes Cymerman, Iwona A. Chung, Inn Beckmann, Benedikt M. Bujnicki, Janusz M. Meiss, Gregor Nucleic Acids Res Nucleic Acid Enzymes Evolutionary conserved mitochondrial nucleases are involved in programmed cell death and normal cell proliferation in lower and higher eukaryotes. The endo/exonuclease Nuc1p, also termed ‘yeast Endonuclease G (EndoG)’, is a member of this class of enzymes that differs from mammalian homologs by the presence of a 5′–3′ exonuclease activity in addition to its broad spectrum endonuclease activity. However, this exonuclease activity is thought to be essential for a function of the yeast enzyme in DNA recombination and repair. Here we show that higher eukaryotes in addition to EndoG contain its paralog ‘EXOG’, a novel EndoG-like mitochondrial endo/exonuclease. We find that during metazoan evolution duplication of an ancestral nuclease gene obviously generated the paralogous EndoG- and EXOG-protein subfamilies in higher eukaryotes, thereby maintaining the full endo/exonuclease activity found in mitochondria of lower eukaryotes. We demonstrate that human EXOG is a dimeric mitochondrial enzyme that displays 5′–3′ exonuclease activity and further differs from EndoG in substrate specificity. We hypothesize that in higher eukaryotes the complementary enzymatic activities of EndoG and EXOG probably together account for both, the lethal and vital functions of conserved mitochondrial endo/exonucleases. Oxford University Press 2008-03 2008-01-10 /pmc/articles/PMC2275078/ /pubmed/18187503 http://dx.doi.org/10.1093/nar/gkm1169 Text en © 2008 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ 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.
spellingShingle Nucleic Acid Enzymes
Cymerman, Iwona A.
Chung, Inn
Beckmann, Benedikt M.
Bujnicki, Janusz M.
Meiss, Gregor
EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title_full EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title_fullStr EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title_full_unstemmed EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title_short EXOG, a novel paralog of Endonuclease G in higher eukaryotes
title_sort exog, a novel paralog of endonuclease g in higher eukaryotes
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2275078/
https://www.ncbi.nlm.nih.gov/pubmed/18187503
http://dx.doi.org/10.1093/nar/gkm1169
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