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A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
Primase‐polymerases (Ppol) are one of the few enzymes able to start DNA synthesis on ssDNA templates. The role of Thermus thermophilus HB27 Ppol, encoded along a putative helicase (Hel) within a mobile genetic element (ICETh2), has been studied. A mutant lacking Ppol showed no effects on the replica...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7693054/ https://www.ncbi.nlm.nih.gov/pubmed/32830367 http://dx.doi.org/10.1111/1462-2920.15207 |
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author | García‐Quintans, Nieves Baquedano, Ignacio Blesa, Alba Verdú, Carlos Berenguer, José Mencía, Mario |
author_facet | García‐Quintans, Nieves Baquedano, Ignacio Blesa, Alba Verdú, Carlos Berenguer, José Mencía, Mario |
author_sort | García‐Quintans, Nieves |
collection | PubMed |
description | Primase‐polymerases (Ppol) are one of the few enzymes able to start DNA synthesis on ssDNA templates. The role of Thermus thermophilus HB27 Ppol, encoded along a putative helicase (Hel) within a mobile genetic element (ICETh2), has been studied. A mutant lacking Ppol showed no effects on the replication of the element. Also, no apparent differences in the sensitivity to DNA damaging agents and other stressors or morphological changes in the mutant cells were detected. However, the mutants lacking Ppol showed an increase in two to three orders of magnitude in their transformation efficiency with plasmids and genomic DNA acquired from the environment (eDNA), independently of its origin and G + C content. In contrast, no significant differences with the wild type were detected when the cells received the DNA from other T. thermophilus partners in conjugation‐like mating experiments. The similarities of this behaviour with that shown by mutants lacking the Argonaute (ThAgo) protein suggests a putative partnership Ppol‐ThAgo in the DNA–DNA interference mechanism of defence, although other eDNA defence mechanisms independent of ThAgo cannot be discarded. |
format | Online Article Text |
id | pubmed-7693054 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-76930542020-12-08 A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA García‐Quintans, Nieves Baquedano, Ignacio Blesa, Alba Verdú, Carlos Berenguer, José Mencía, Mario Environ Microbiol Research Articles Primase‐polymerases (Ppol) are one of the few enzymes able to start DNA synthesis on ssDNA templates. The role of Thermus thermophilus HB27 Ppol, encoded along a putative helicase (Hel) within a mobile genetic element (ICETh2), has been studied. A mutant lacking Ppol showed no effects on the replication of the element. Also, no apparent differences in the sensitivity to DNA damaging agents and other stressors or morphological changes in the mutant cells were detected. However, the mutants lacking Ppol showed an increase in two to three orders of magnitude in their transformation efficiency with plasmids and genomic DNA acquired from the environment (eDNA), independently of its origin and G + C content. In contrast, no significant differences with the wild type were detected when the cells received the DNA from other T. thermophilus partners in conjugation‐like mating experiments. The similarities of this behaviour with that shown by mutants lacking the Argonaute (ThAgo) protein suggests a putative partnership Ppol‐ThAgo in the DNA–DNA interference mechanism of defence, although other eDNA defence mechanisms independent of ThAgo cannot be discarded. John Wiley & Sons, Inc. 2020-09-03 2020-11 /pmc/articles/PMC7693054/ /pubmed/32830367 http://dx.doi.org/10.1111/1462-2920.15207 Text en © 2020 The Authors. Environmental Microbiology published by Society for Applied Microbiology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles García‐Quintans, Nieves Baquedano, Ignacio Blesa, Alba Verdú, Carlos Berenguer, José Mencía, Mario A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA |
title | A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
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title_full | A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
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title_fullStr | A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
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title_full_unstemmed | A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
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title_short | A thermostable DNA primase‐polymerase from a mobile genetic element involved in defence against environmental DNA
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title_sort | thermostable dna primase‐polymerase from a mobile genetic element involved in defence against environmental dna |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7693054/ https://www.ncbi.nlm.nih.gov/pubmed/32830367 http://dx.doi.org/10.1111/1462-2920.15207 |
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