The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.

Loss of amino groups from adenines in DNA results in the formation of hypoxanthine (Hx) bases with miscoding properties. The primary enzyme in Escherichia coli for DNA repair initiation at deaminated adenine is endonuclease V (endoV), encoded by the nfi gene, which cleaves the second phosphodiester...

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Autores principales:	Cathrine Fladeby, Erik Sebastian Vik, Jon K Laerdahl, Christine Gran Neurauter, Julie E Heggelund, Eirik Thorgaard, Pernille Strøm-Andersen, Magnar Bjørås, Bjørn Dalhus, Ingrun Alseth
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/bb426f79ed904e0cb7f206bd3e15855d
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spelling	oai:doaj.org-article:bb426f79ed904e0cb7f206bd3e15855d2021-11-18T08:10:07ZThe human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.1932-620310.1371/journal.pone.0047466https://doaj.org/article/bb426f79ed904e0cb7f206bd3e15855d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23139746/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Loss of amino groups from adenines in DNA results in the formation of hypoxanthine (Hx) bases with miscoding properties. The primary enzyme in Escherichia coli for DNA repair initiation at deaminated adenine is endonuclease V (endoV), encoded by the nfi gene, which cleaves the second phosphodiester bond 3' of an Hx lesion. Endonuclease V orthologs are widespread in nature and belong to a family of highly conserved proteins. Whereas prokaryotic endoV enzymes are well characterized, the function of the eukaryotic homologs remains obscure. Here we describe the human endoV ortholog and show with bioinformatics and experimental analysis that a large number of transcript variants exist for the human endonuclease V gene (ENDOV), many of which are unlikely to be translated into functional protein. Full-length ENDOV is encoded by 8 evolutionary conserved exons covering the core region of the enzyme, in addition to one or more 3'-exons encoding an unstructured and poorly conserved C-terminus. In contrast to the E. coli enzyme, we find recombinant ENDOV neither to incise nor bind Hx-containing DNA. While both enzymes have strong affinity for several branched DNA substrates, cleavage is observed only with E. coli endoV. We find that ENDOV is localized in the cytoplasm and nucleoli of human cells. As nucleoli harbor the rRNA genes, this may suggest a role for the protein in rRNA gene transactions such as DNA replication or RNA transcription.Cathrine FladebyErik Sebastian VikJon K LaerdahlChristine Gran NeurauterJulie E HeggelundEirik ThorgaardPernille Strøm-AndersenMagnar BjøråsBjørn DalhusIngrun AlsethPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 11, p e47466 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Cathrine Fladeby Erik Sebastian Vik Jon K Laerdahl Christine Gran Neurauter Julie E Heggelund Eirik Thorgaard Pernille Strøm-Andersen Magnar Bjørås Bjørn Dalhus Ingrun Alseth The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
description	Loss of amino groups from adenines in DNA results in the formation of hypoxanthine (Hx) bases with miscoding properties. The primary enzyme in Escherichia coli for DNA repair initiation at deaminated adenine is endonuclease V (endoV), encoded by the nfi gene, which cleaves the second phosphodiester bond 3' of an Hx lesion. Endonuclease V orthologs are widespread in nature and belong to a family of highly conserved proteins. Whereas prokaryotic endoV enzymes are well characterized, the function of the eukaryotic homologs remains obscure. Here we describe the human endoV ortholog and show with bioinformatics and experimental analysis that a large number of transcript variants exist for the human endonuclease V gene (ENDOV), many of which are unlikely to be translated into functional protein. Full-length ENDOV is encoded by 8 evolutionary conserved exons covering the core region of the enzyme, in addition to one or more 3'-exons encoding an unstructured and poorly conserved C-terminus. In contrast to the E. coli enzyme, we find recombinant ENDOV neither to incise nor bind Hx-containing DNA. While both enzymes have strong affinity for several branched DNA substrates, cleavage is observed only with E. coli endoV. We find that ENDOV is localized in the cytoplasm and nucleoli of human cells. As nucleoli harbor the rRNA genes, this may suggest a role for the protein in rRNA gene transactions such as DNA replication or RNA transcription.
format	article
author	Cathrine Fladeby Erik Sebastian Vik Jon K Laerdahl Christine Gran Neurauter Julie E Heggelund Eirik Thorgaard Pernille Strøm-Andersen Magnar Bjørås Bjørn Dalhus Ingrun Alseth
author_facet	Cathrine Fladeby Erik Sebastian Vik Jon K Laerdahl Christine Gran Neurauter Julie E Heggelund Eirik Thorgaard Pernille Strøm-Andersen Magnar Bjørås Bjørn Dalhus Ingrun Alseth
author_sort	Cathrine Fladeby
title	The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
title_short	The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
title_full	The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
title_fullStr	The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
title_full_unstemmed	The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.
title_sort	human homolog of escherichia coli endonuclease v is a nucleolar protein with affinity for branched dna structures.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/bb426f79ed904e0cb7f206bd3e15855d
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The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures.

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