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Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions
The majority of DNA polymerases (DNAPs) are specialized enzymes with specific roles in DNA replication, translesion DNA synthesis (TLS), or DNA repair. The enzymatic characteristics to perform accurate DNA replication are in apparent contradiction with TLS or DNA repair abilities. For instance, repl...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699545/ https://www.ncbi.nlm.nih.gov/pubmed/33228188 http://dx.doi.org/10.3390/genes11111370 |
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author | Peralta-Castro, Antolín García-Medel, Paola L. Baruch-Torres, Noe Trasviña-Arenas, Carlos H. Juarez-Quintero, Víctor Morales-Vazquez, Carlos M. Brieba, Luis G. |
author_facet | Peralta-Castro, Antolín García-Medel, Paola L. Baruch-Torres, Noe Trasviña-Arenas, Carlos H. Juarez-Quintero, Víctor Morales-Vazquez, Carlos M. Brieba, Luis G. |
author_sort | Peralta-Castro, Antolín |
collection | PubMed |
description | The majority of DNA polymerases (DNAPs) are specialized enzymes with specific roles in DNA replication, translesion DNA synthesis (TLS), or DNA repair. The enzymatic characteristics to perform accurate DNA replication are in apparent contradiction with TLS or DNA repair abilities. For instance, replicative DNAPs incorporate nucleotides with high fidelity and processivity, whereas TLS DNAPs are low-fidelity polymerases with distributive nucleotide incorporation. Plant organelles (mitochondria and chloroplast) are replicated by family-A DNA polymerases that are both replicative and TLS DNAPs. Furthermore, plant organellar DNA polymerases from the plant model Arabidopsis thaliana (AtPOLIs) execute repair of double-stranded breaks by microhomology-mediated end-joining and perform Base Excision Repair (BER) using lyase and strand-displacement activities. AtPOLIs harbor three unique insertions in their polymerization domain that are associated with TLS, microhomology-mediated end-joining (MMEJ), strand-displacement, and lyase activities. We postulate that AtPOLIs are able to execute those different functions through the acquisition of these novel amino acid insertions, making them multifunctional enzymes able to participate in DNA replication and DNA repair. |
format | Online Article Text |
id | pubmed-7699545 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76995452020-11-29 Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions Peralta-Castro, Antolín García-Medel, Paola L. Baruch-Torres, Noe Trasviña-Arenas, Carlos H. Juarez-Quintero, Víctor Morales-Vazquez, Carlos M. Brieba, Luis G. Genes (Basel) Review The majority of DNA polymerases (DNAPs) are specialized enzymes with specific roles in DNA replication, translesion DNA synthesis (TLS), or DNA repair. The enzymatic characteristics to perform accurate DNA replication are in apparent contradiction with TLS or DNA repair abilities. For instance, replicative DNAPs incorporate nucleotides with high fidelity and processivity, whereas TLS DNAPs are low-fidelity polymerases with distributive nucleotide incorporation. Plant organelles (mitochondria and chloroplast) are replicated by family-A DNA polymerases that are both replicative and TLS DNAPs. Furthermore, plant organellar DNA polymerases from the plant model Arabidopsis thaliana (AtPOLIs) execute repair of double-stranded breaks by microhomology-mediated end-joining and perform Base Excision Repair (BER) using lyase and strand-displacement activities. AtPOLIs harbor three unique insertions in their polymerization domain that are associated with TLS, microhomology-mediated end-joining (MMEJ), strand-displacement, and lyase activities. We postulate that AtPOLIs are able to execute those different functions through the acquisition of these novel amino acid insertions, making them multifunctional enzymes able to participate in DNA replication and DNA repair. MDPI 2020-11-19 /pmc/articles/PMC7699545/ /pubmed/33228188 http://dx.doi.org/10.3390/genes11111370 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Peralta-Castro, Antolín García-Medel, Paola L. Baruch-Torres, Noe Trasviña-Arenas, Carlos H. Juarez-Quintero, Víctor Morales-Vazquez, Carlos M. Brieba, Luis G. Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title | Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title_full | Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title_fullStr | Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title_full_unstemmed | Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title_short | Plant Organellar DNA Polymerases Evolved Multifunctionality through the Acquisition of Novel Amino Acid Insertions |
title_sort | plant organellar dna polymerases evolved multifunctionality through the acquisition of novel amino acid insertions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7699545/ https://www.ncbi.nlm.nih.gov/pubmed/33228188 http://dx.doi.org/10.3390/genes11111370 |
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