A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol.
BACKGROUND: Eukaryotic family A DNA polymerases are involved in mitochondrial DNA replication or translesion DNA synthesis. Here, we present evidence that the sole family A DNA polymerase from the parasite protozoan E. histolytica (EhDNApolA) localizes to the nucleus and that its biochemical propert...
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ftdoajarticles:oai:doaj.org/article:7c066069e18044fab6c264dcc92bb1ab 2023-05-15T15:08:27+02:00 A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. Guillermo Pastor-Palacios Elisa Azuara-Liceaga Luis G Brieba 2010-01-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0000786 https://doaj.org/article/7c066069e18044fab6c264dcc92bb1ab EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC2919377?pdf=render https://doaj.org/toc/1935-2735 1935-2735 doi:10.1371/journal.pntd.0000786 https://doaj.org/article/7c066069e18044fab6c264dcc92bb1ab PLoS Neglected Tropical Diseases, Vol 4, Iss 8, p e786 (2010) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2010 ftdoajarticles https://doi.org/10.1371/journal.pntd.0000786 2022-12-31T12:49:24Z BACKGROUND: Eukaryotic family A DNA polymerases are involved in mitochondrial DNA replication or translesion DNA synthesis. Here, we present evidence that the sole family A DNA polymerase from the parasite protozoan E. histolytica (EhDNApolA) localizes to the nucleus and that its biochemical properties indicate that this DNA polymerase may be involved in translesion DNA synthesis. METHODOLOGY AND RESULTS: EhDNApolA is the sole family A DNA polymerase in E. histolytica. An in silico analysis places family A DNA polymerases from the genus Entamoeba in a separate branch of a family A DNA polymerases phylogenetic tree. Biochemical studies of a purified recombinant EhDNApolA demonstrated that this polymerase is active in primer elongation, is poorly processive, displays moderate strand displacement, and does not contain 3'-5' exonuclease or editing activity. Importantly, EhDNApolA bypasses thymine glycol lesions with high fidelity, and confocal microscopy demonstrates that this polymerase is translocated into the nucleus. These data suggest a putative role of EhDNApolA in translesion DNA synthesis in E. histolytica. CONCLUSION: This is the first report of the biochemical characterization of a DNA polymerase from E. histolytica. EhDNApolA is a family A DNA polymerase that is grouped into a new subfamily of DNA polymerases with translesion DNA synthesis capabilities similar to DNA polymerases from subfamily nu. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLoS Neglected Tropical Diseases 4 8 e786 |
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Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
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English |
topic |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Guillermo Pastor-Palacios Elisa Azuara-Liceaga Luis G Brieba A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
BACKGROUND: Eukaryotic family A DNA polymerases are involved in mitochondrial DNA replication or translesion DNA synthesis. Here, we present evidence that the sole family A DNA polymerase from the parasite protozoan E. histolytica (EhDNApolA) localizes to the nucleus and that its biochemical properties indicate that this DNA polymerase may be involved in translesion DNA synthesis. METHODOLOGY AND RESULTS: EhDNApolA is the sole family A DNA polymerase in E. histolytica. An in silico analysis places family A DNA polymerases from the genus Entamoeba in a separate branch of a family A DNA polymerases phylogenetic tree. Biochemical studies of a purified recombinant EhDNApolA demonstrated that this polymerase is active in primer elongation, is poorly processive, displays moderate strand displacement, and does not contain 3'-5' exonuclease or editing activity. Importantly, EhDNApolA bypasses thymine glycol lesions with high fidelity, and confocal microscopy demonstrates that this polymerase is translocated into the nucleus. These data suggest a putative role of EhDNApolA in translesion DNA synthesis in E. histolytica. CONCLUSION: This is the first report of the biochemical characterization of a DNA polymerase from E. histolytica. EhDNApolA is a family A DNA polymerase that is grouped into a new subfamily of DNA polymerases with translesion DNA synthesis capabilities similar to DNA polymerases from subfamily nu. |
format |
Article in Journal/Newspaper |
author |
Guillermo Pastor-Palacios Elisa Azuara-Liceaga Luis G Brieba |
author_facet |
Guillermo Pastor-Palacios Elisa Azuara-Liceaga Luis G Brieba |
author_sort |
Guillermo Pastor-Palacios |
title |
A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
title_short |
A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
title_full |
A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
title_fullStr |
A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
title_full_unstemmed |
A nuclear family A DNA polymerase from Entamoeba histolytica bypasses thymine glycol. |
title_sort |
nuclear family a dna polymerase from entamoeba histolytica bypasses thymine glycol. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2010 |
url |
https://doi.org/10.1371/journal.pntd.0000786 https://doaj.org/article/7c066069e18044fab6c264dcc92bb1ab |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 4, Iss 8, p e786 (2010) |
op_relation |
http://europepmc.org/articles/PMC2919377?pdf=render https://doaj.org/toc/1935-2735 1935-2735 doi:10.1371/journal.pntd.0000786 https://doaj.org/article/7c066069e18044fab6c264dcc92bb1ab |
op_doi |
https://doi.org/10.1371/journal.pntd.0000786 |
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PLoS Neglected Tropical Diseases |
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4 |
container_issue |
8 |
container_start_page |
e786 |
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1766339816320925696 |