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A Prokaryotic Twist on Argonaute Function

Argonaute proteins can be found in all three domains of life. In eukaryotic organisms, Argonaute is, as the functional core of the RNA-silencing machinery, critically involved in the regulation of gene expression. Despite the mechanistic and structural similarities between archaeal, bacterial and eu...

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Detalles Bibliográficos
Autores principales: Willkomm, Sarah, Zander, Adrian, Gust, Alexander, Grohmann, Dina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390867/
https://www.ncbi.nlm.nih.gov/pubmed/25692904
http://dx.doi.org/10.3390/life5010538
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author Willkomm, Sarah
Zander, Adrian
Gust, Alexander
Grohmann, Dina
author_facet Willkomm, Sarah
Zander, Adrian
Gust, Alexander
Grohmann, Dina
author_sort Willkomm, Sarah
collection PubMed
description Argonaute proteins can be found in all three domains of life. In eukaryotic organisms, Argonaute is, as the functional core of the RNA-silencing machinery, critically involved in the regulation of gene expression. Despite the mechanistic and structural similarities between archaeal, bacterial and eukaryotic Argonaute proteins, the biological function of bacterial and archaeal Argonautes has remained elusive. This review discusses new findings in the field that shed light on the structure and function of Argonaute. We especially focus on archaeal Argonautes when discussing the details of the structural and dynamic features in Argonaute that promote substrate recognition and cleavage, thereby revealing differences and similarities in Argonaute biology.
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spelling pubmed-43908672015-05-21 A Prokaryotic Twist on Argonaute Function Willkomm, Sarah Zander, Adrian Gust, Alexander Grohmann, Dina Life (Basel) Review Argonaute proteins can be found in all three domains of life. In eukaryotic organisms, Argonaute is, as the functional core of the RNA-silencing machinery, critically involved in the regulation of gene expression. Despite the mechanistic and structural similarities between archaeal, bacterial and eukaryotic Argonaute proteins, the biological function of bacterial and archaeal Argonautes has remained elusive. This review discusses new findings in the field that shed light on the structure and function of Argonaute. We especially focus on archaeal Argonautes when discussing the details of the structural and dynamic features in Argonaute that promote substrate recognition and cleavage, thereby revealing differences and similarities in Argonaute biology. MDPI 2015-02-16 /pmc/articles/PMC4390867/ /pubmed/25692904 http://dx.doi.org/10.3390/life5010538 Text en © 2015 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 license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Willkomm, Sarah
Zander, Adrian
Gust, Alexander
Grohmann, Dina
A Prokaryotic Twist on Argonaute Function
title A Prokaryotic Twist on Argonaute Function
title_full A Prokaryotic Twist on Argonaute Function
title_fullStr A Prokaryotic Twist on Argonaute Function
title_full_unstemmed A Prokaryotic Twist on Argonaute Function
title_short A Prokaryotic Twist on Argonaute Function
title_sort prokaryotic twist on argonaute function
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390867/
https://www.ncbi.nlm.nih.gov/pubmed/25692904
http://dx.doi.org/10.3390/life5010538
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