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The Expanded Universe of Prokaryotic Argonaute Proteins
Members of the ancient family of Argonaute (Ago) proteins are present in all domains of life. The common feature of Ago proteins is the ability to bind small nucleic acid guides and use them for sequence-specific recognition—and sometimes cleavage—of complementary targets. While eukaryotic Ago (eAgo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6299218/ https://www.ncbi.nlm.nih.gov/pubmed/30563906 http://dx.doi.org/10.1128/mBio.01935-18 |
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author | Ryazansky, Sergei Kulbachinskiy, Andrey Aravin, Alexei A. |
author_facet | Ryazansky, Sergei Kulbachinskiy, Andrey Aravin, Alexei A. |
author_sort | Ryazansky, Sergei |
collection | PubMed |
description | Members of the ancient family of Argonaute (Ago) proteins are present in all domains of life. The common feature of Ago proteins is the ability to bind small nucleic acid guides and use them for sequence-specific recognition—and sometimes cleavage—of complementary targets. While eukaryotic Ago (eAgo) proteins are key players in RNA interference and related pathways, the properties and functions of these proteins in archaeal and bacterial species have just started to emerge. We undertook comprehensive exploration of prokaryotic Ago (pAgo) proteins in sequenced genomes and revealed their striking diversity in comparison with eAgos. Many pAgos contain divergent variants of the conserved domains involved in interactions with nucleic acids, while having extra domains that are absent in eAgos, suggesting that they might have unusual specificities in the nucleic acid recognition and cleavage. Many pAgos are associated with putative nucleases, helicases, and DNA binding proteins in the same gene or operon, suggesting that they are involved in target processing. The great variability of pAgos revealed by our analysis opens new ways for exploration of their functions in host cells and for their use as potential tools in genome editing. |
format | Online Article Text |
id | pubmed-6299218 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | American Society for Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-62992182018-12-28 The Expanded Universe of Prokaryotic Argonaute Proteins Ryazansky, Sergei Kulbachinskiy, Andrey Aravin, Alexei A. mBio Research Article Members of the ancient family of Argonaute (Ago) proteins are present in all domains of life. The common feature of Ago proteins is the ability to bind small nucleic acid guides and use them for sequence-specific recognition—and sometimes cleavage—of complementary targets. While eukaryotic Ago (eAgo) proteins are key players in RNA interference and related pathways, the properties and functions of these proteins in archaeal and bacterial species have just started to emerge. We undertook comprehensive exploration of prokaryotic Ago (pAgo) proteins in sequenced genomes and revealed their striking diversity in comparison with eAgos. Many pAgos contain divergent variants of the conserved domains involved in interactions with nucleic acids, while having extra domains that are absent in eAgos, suggesting that they might have unusual specificities in the nucleic acid recognition and cleavage. Many pAgos are associated with putative nucleases, helicases, and DNA binding proteins in the same gene or operon, suggesting that they are involved in target processing. The great variability of pAgos revealed by our analysis opens new ways for exploration of their functions in host cells and for their use as potential tools in genome editing. American Society for Microbiology 2018-12-18 /pmc/articles/PMC6299218/ /pubmed/30563906 http://dx.doi.org/10.1128/mBio.01935-18 Text en Copyright © 2018 Ryazansky et al. https://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research Article Ryazansky, Sergei Kulbachinskiy, Andrey Aravin, Alexei A. The Expanded Universe of Prokaryotic Argonaute Proteins |
title | The Expanded Universe of Prokaryotic Argonaute Proteins |
title_full | The Expanded Universe of Prokaryotic Argonaute Proteins |
title_fullStr | The Expanded Universe of Prokaryotic Argonaute Proteins |
title_full_unstemmed | The Expanded Universe of Prokaryotic Argonaute Proteins |
title_short | The Expanded Universe of Prokaryotic Argonaute Proteins |
title_sort | expanded universe of prokaryotic argonaute proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6299218/ https://www.ncbi.nlm.nih.gov/pubmed/30563906 http://dx.doi.org/10.1128/mBio.01935-18 |
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