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Revealing a new activity of the human Dicer DUF283 domain in vitro

The ribonuclease Dicer is a multidomain enzyme that plays a fundamental role in the biogenesis of small regulatory RNAs (srRNAs), which control gene expression by targeting complementary transcripts and inducing their cleavage or repressing their translation. Recent studies of Dicer’s domains have p...

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Autores principales: Kurzynska-Kokorniak, Anna, Pokornowska, Maria, Koralewska, Natalia, Hoffmann, Weronika, Bienkowska-Szewczyk, Krystyna, Figlerowicz, Marek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4820750/
https://www.ncbi.nlm.nih.gov/pubmed/27045313
http://dx.doi.org/10.1038/srep23989
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author Kurzynska-Kokorniak, Anna
Pokornowska, Maria
Koralewska, Natalia
Hoffmann, Weronika
Bienkowska-Szewczyk, Krystyna
Figlerowicz, Marek
author_facet Kurzynska-Kokorniak, Anna
Pokornowska, Maria
Koralewska, Natalia
Hoffmann, Weronika
Bienkowska-Szewczyk, Krystyna
Figlerowicz, Marek
author_sort Kurzynska-Kokorniak, Anna
collection PubMed
description The ribonuclease Dicer is a multidomain enzyme that plays a fundamental role in the biogenesis of small regulatory RNAs (srRNAs), which control gene expression by targeting complementary transcripts and inducing their cleavage or repressing their translation. Recent studies of Dicer’s domains have permitted to propose their roles in srRNA biogenesis. For all of Dicer’s domains except one, called DUF283 (domain of unknown function), their involvement in RNA substrate recognition, binding or cleavage has been postulated. For DUF283, the interaction with Dicer’s protein partners has been the only function suggested thus far. In this report, we demonstrate that the isolated DUF283 domain from human Dicer is capable of binding single-stranded nucleic acids in vitro. We also show that DUF283 can act as a nucleic acid annealer that accelerates base-pairing between complementary RNA/DNA molecules in vitro. We further demonstrate an annealing activity of full length human Dicer. The overall results suggest that Dicer, presumably through its DUF283 domain, might facilitate hybridization between short RNAs and their targets. The presented findings reveal the complex nature of Dicer, whose functions may extend beyond the biogenesis of srRNAs.
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spelling pubmed-48207502016-04-06 Revealing a new activity of the human Dicer DUF283 domain in vitro Kurzynska-Kokorniak, Anna Pokornowska, Maria Koralewska, Natalia Hoffmann, Weronika Bienkowska-Szewczyk, Krystyna Figlerowicz, Marek Sci Rep Article The ribonuclease Dicer is a multidomain enzyme that plays a fundamental role in the biogenesis of small regulatory RNAs (srRNAs), which control gene expression by targeting complementary transcripts and inducing their cleavage or repressing their translation. Recent studies of Dicer’s domains have permitted to propose their roles in srRNA biogenesis. For all of Dicer’s domains except one, called DUF283 (domain of unknown function), their involvement in RNA substrate recognition, binding or cleavage has been postulated. For DUF283, the interaction with Dicer’s protein partners has been the only function suggested thus far. In this report, we demonstrate that the isolated DUF283 domain from human Dicer is capable of binding single-stranded nucleic acids in vitro. We also show that DUF283 can act as a nucleic acid annealer that accelerates base-pairing between complementary RNA/DNA molecules in vitro. We further demonstrate an annealing activity of full length human Dicer. The overall results suggest that Dicer, presumably through its DUF283 domain, might facilitate hybridization between short RNAs and their targets. The presented findings reveal the complex nature of Dicer, whose functions may extend beyond the biogenesis of srRNAs. Nature Publishing Group 2016-04-05 /pmc/articles/PMC4820750/ /pubmed/27045313 http://dx.doi.org/10.1038/srep23989 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Kurzynska-Kokorniak, Anna
Pokornowska, Maria
Koralewska, Natalia
Hoffmann, Weronika
Bienkowska-Szewczyk, Krystyna
Figlerowicz, Marek
Revealing a new activity of the human Dicer DUF283 domain in vitro
title Revealing a new activity of the human Dicer DUF283 domain in vitro
title_full Revealing a new activity of the human Dicer DUF283 domain in vitro
title_fullStr Revealing a new activity of the human Dicer DUF283 domain in vitro
title_full_unstemmed Revealing a new activity of the human Dicer DUF283 domain in vitro
title_short Revealing a new activity of the human Dicer DUF283 domain in vitro
title_sort revealing a new activity of the human dicer duf283 domain in vitro
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4820750/
https://www.ncbi.nlm.nih.gov/pubmed/27045313
http://dx.doi.org/10.1038/srep23989
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