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RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly
P-bodies (PBs) are cytoplasmic mRNA-protein (mRNP) granules conserved throughout eukaryotes which are implicated in the repression, storage and degradation of mRNAs. PB assembly is driven by proteins with self-interacting and low-complexity domains. Non-translating mRNA also stimulates PB assembly,...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7293044/ https://www.ncbi.nlm.nih.gov/pubmed/32396167 http://dx.doi.org/10.1093/nar/gkaa352 |
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author | Fernandes, Nikita Buchan, J Ross |
author_facet | Fernandes, Nikita Buchan, J Ross |
author_sort | Fernandes, Nikita |
collection | PubMed |
description | P-bodies (PBs) are cytoplasmic mRNA-protein (mRNP) granules conserved throughout eukaryotes which are implicated in the repression, storage and degradation of mRNAs. PB assembly is driven by proteins with self-interacting and low-complexity domains. Non-translating mRNA also stimulates PB assembly, however no studies to date have explored whether particular mRNA transcripts are more critical than others in facilitating PB assembly. Previous work revealed that rps28bΔ (small ribosomal subunit-28B) mutants do not form PBs under normal growth conditions. Here, we demonstrate that the RPS28B 3′UTR is important for PB assembly, consistent with it harboring a binding site for the PB assembly protein Edc3. However, expression of the RPS28B 3′UTR alone is insufficient to drive PB assembly. Intriguingly, chimeric mRNA studies revealed that Rps28 protein, translated in cis from an mRNA bearing the RPS28B 3′UTR, physically interacts more strongly with Edc3 than Rps28 protein synthesized in trans. This Edc3-Rps28 interaction in turn facilitates PB assembly. Our work indicates that PB assembly may be nucleated by specific RNA ‘scaffolds’. Furthermore, this is the first description in yeast to our knowledge of a cis-translated protein interacting with another protein in the 3′UTR of the mRNA which encoded it, which in turn stimulates assembly of cellular structures. |
format | Online Article Text |
id | pubmed-7293044 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-72930442020-06-17 RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly Fernandes, Nikita Buchan, J Ross Nucleic Acids Res RNA and RNA-protein complexes P-bodies (PBs) are cytoplasmic mRNA-protein (mRNP) granules conserved throughout eukaryotes which are implicated in the repression, storage and degradation of mRNAs. PB assembly is driven by proteins with self-interacting and low-complexity domains. Non-translating mRNA also stimulates PB assembly, however no studies to date have explored whether particular mRNA transcripts are more critical than others in facilitating PB assembly. Previous work revealed that rps28bΔ (small ribosomal subunit-28B) mutants do not form PBs under normal growth conditions. Here, we demonstrate that the RPS28B 3′UTR is important for PB assembly, consistent with it harboring a binding site for the PB assembly protein Edc3. However, expression of the RPS28B 3′UTR alone is insufficient to drive PB assembly. Intriguingly, chimeric mRNA studies revealed that Rps28 protein, translated in cis from an mRNA bearing the RPS28B 3′UTR, physically interacts more strongly with Edc3 than Rps28 protein synthesized in trans. This Edc3-Rps28 interaction in turn facilitates PB assembly. Our work indicates that PB assembly may be nucleated by specific RNA ‘scaffolds’. Furthermore, this is the first description in yeast to our knowledge of a cis-translated protein interacting with another protein in the 3′UTR of the mRNA which encoded it, which in turn stimulates assembly of cellular structures. Oxford University Press 2020-06-19 2020-05-12 /pmc/articles/PMC7293044/ /pubmed/32396167 http://dx.doi.org/10.1093/nar/gkaa352 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | RNA and RNA-protein complexes Fernandes, Nikita Buchan, J Ross RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title |
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title_full |
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title_fullStr |
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title_full_unstemmed |
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title_short |
RPS28B mRNA acts as a scaffold promoting cis-translational interaction of proteins driving P-body assembly |
title_sort | rps28b mrna acts as a scaffold promoting cis-translational interaction of proteins driving p-body assembly |
topic | RNA and RNA-protein complexes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7293044/ https://www.ncbi.nlm.nih.gov/pubmed/32396167 http://dx.doi.org/10.1093/nar/gkaa352 |
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