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RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis
The RNA exosome is a key 3’−5’ exoribonuclease with an evolutionarily conserved structure and function. Its cytosolic functions require the co-factors SKI7 and the Ski complex. Here we demonstrate by co-purification experiments that the ARM-repeat protein RESURRECTION1 (RST1) and RST1 INTERACTING PR...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6711988/ https://www.ncbi.nlm.nih.gov/pubmed/31455787 http://dx.doi.org/10.1038/s41467-019-11807-4 |
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author | Lange, Heike Ndecky, Simon Y. A. Gomez-Diaz, Carlos Pflieger, David Butel, Nicolas Zumsteg, Julie Kuhn, Lauriane Piermaria, Christina Chicher, Johana Christie, Michael Karaaslan, Ezgi S. Lang, Patricia L. M. Weigel, Detlef Vaucheret, Hervé Hammann, Philippe Gagliardi, Dominique |
author_facet | Lange, Heike Ndecky, Simon Y. A. Gomez-Diaz, Carlos Pflieger, David Butel, Nicolas Zumsteg, Julie Kuhn, Lauriane Piermaria, Christina Chicher, Johana Christie, Michael Karaaslan, Ezgi S. Lang, Patricia L. M. Weigel, Detlef Vaucheret, Hervé Hammann, Philippe Gagliardi, Dominique |
author_sort | Lange, Heike |
collection | PubMed |
description | The RNA exosome is a key 3’−5’ exoribonuclease with an evolutionarily conserved structure and function. Its cytosolic functions require the co-factors SKI7 and the Ski complex. Here we demonstrate by co-purification experiments that the ARM-repeat protein RESURRECTION1 (RST1) and RST1 INTERACTING PROTEIN (RIPR) connect the cytosolic Arabidopsis RNA exosome to the Ski complex. rst1 and ripr mutants accumulate RNA quality control siRNAs (rqc-siRNAs) produced by the post-transcriptional gene silencing (PTGS) machinery when mRNA degradation is compromised. The small RNA populations observed in rst1 and ripr mutants are also detected in mutants lacking the RRP45B/CER7 core exosome subunit. Thus, molecular and genetic evidence supports a physical and functional link between RST1, RIPR and the RNA exosome. Our data reveal the existence of additional cytosolic exosome co-factors besides the known Ski subunits. RST1 is not restricted to plants, as homologues with a similar domain architecture but unknown function exist in animals, including humans. |
format | Online Article Text |
id | pubmed-6711988 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-67119882019-08-29 RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis Lange, Heike Ndecky, Simon Y. A. Gomez-Diaz, Carlos Pflieger, David Butel, Nicolas Zumsteg, Julie Kuhn, Lauriane Piermaria, Christina Chicher, Johana Christie, Michael Karaaslan, Ezgi S. Lang, Patricia L. M. Weigel, Detlef Vaucheret, Hervé Hammann, Philippe Gagliardi, Dominique Nat Commun Article The RNA exosome is a key 3’−5’ exoribonuclease with an evolutionarily conserved structure and function. Its cytosolic functions require the co-factors SKI7 and the Ski complex. Here we demonstrate by co-purification experiments that the ARM-repeat protein RESURRECTION1 (RST1) and RST1 INTERACTING PROTEIN (RIPR) connect the cytosolic Arabidopsis RNA exosome to the Ski complex. rst1 and ripr mutants accumulate RNA quality control siRNAs (rqc-siRNAs) produced by the post-transcriptional gene silencing (PTGS) machinery when mRNA degradation is compromised. The small RNA populations observed in rst1 and ripr mutants are also detected in mutants lacking the RRP45B/CER7 core exosome subunit. Thus, molecular and genetic evidence supports a physical and functional link between RST1, RIPR and the RNA exosome. Our data reveal the existence of additional cytosolic exosome co-factors besides the known Ski subunits. RST1 is not restricted to plants, as homologues with a similar domain architecture but unknown function exist in animals, including humans. Nature Publishing Group UK 2019-08-27 /pmc/articles/PMC6711988/ /pubmed/31455787 http://dx.doi.org/10.1038/s41467-019-11807-4 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Lange, Heike Ndecky, Simon Y. A. Gomez-Diaz, Carlos Pflieger, David Butel, Nicolas Zumsteg, Julie Kuhn, Lauriane Piermaria, Christina Chicher, Johana Christie, Michael Karaaslan, Ezgi S. Lang, Patricia L. M. Weigel, Detlef Vaucheret, Hervé Hammann, Philippe Gagliardi, Dominique RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title | RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title_full | RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title_fullStr | RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title_full_unstemmed | RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title_short | RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis |
title_sort | rst1 and ripr connect the cytosolic rna exosome to the ski complex in arabidopsis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6711988/ https://www.ncbi.nlm.nih.gov/pubmed/31455787 http://dx.doi.org/10.1038/s41467-019-11807-4 |
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