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Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing
The nuclear structures that contain symmetrical dimethylated arginine (sDMA)–modified proteins and the role of this posttranslational modification is unknown. Here we report that the Cajal body is a major epitope in HeLa cells for an sDMA-specific antibody and that coilin is an sDMA-containing prote...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173973/ https://www.ncbi.nlm.nih.gov/pubmed/12486110 http://dx.doi.org/10.1083/jcb.200207028 |
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author | Boisvert, François-Michel Côté, Jocelyn Boulanger, Marie-Chloé Cléroux, Patrick Bachand, François Autexier, Chantal Richard, Stéphane |
author_facet | Boisvert, François-Michel Côté, Jocelyn Boulanger, Marie-Chloé Cléroux, Patrick Bachand, François Autexier, Chantal Richard, Stéphane |
author_sort | Boisvert, François-Michel |
collection | PubMed |
description | The nuclear structures that contain symmetrical dimethylated arginine (sDMA)–modified proteins and the role of this posttranslational modification is unknown. Here we report that the Cajal body is a major epitope in HeLa cells for an sDMA-specific antibody and that coilin is an sDMA-containing protein as analyzed by using the sDMA-specific antibody and matrix-assisted laser desorption ionization time of flight mass spectrometry. The methylation inhibitor 5′-deoxy-5′-methylthioadenosine reduces the levels of coilin methylation and causes the appearance of SMN-positive gems. In cells devoid of Cajal bodies, such as primary fibroblasts, sDMA-containing proteins concentrated in speckles. Cells from a patient with spinal muscular atrophy, containing low levels of the methyl-binding protein SMN, localized sDMA-containing proteins in the nucleoplasm as a discrete granular pattern. Splicing reactions are efficiently inhibited by using the sDMA-specific antibody or by using hypomethylated nuclear extracts, showing that active spliceosomes contain sDMA polypeptides and suggesting that arginine methylation is important for efficient pre-mRNA splicing. Our findings support a model in which arginine methylation is important for the localization of coilin and SMN in Cajal bodies. |
format | Text |
id | pubmed-2173973 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21739732008-05-01 Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing Boisvert, François-Michel Côté, Jocelyn Boulanger, Marie-Chloé Cléroux, Patrick Bachand, François Autexier, Chantal Richard, Stéphane J Cell Biol Article The nuclear structures that contain symmetrical dimethylated arginine (sDMA)–modified proteins and the role of this posttranslational modification is unknown. Here we report that the Cajal body is a major epitope in HeLa cells for an sDMA-specific antibody and that coilin is an sDMA-containing protein as analyzed by using the sDMA-specific antibody and matrix-assisted laser desorption ionization time of flight mass spectrometry. The methylation inhibitor 5′-deoxy-5′-methylthioadenosine reduces the levels of coilin methylation and causes the appearance of SMN-positive gems. In cells devoid of Cajal bodies, such as primary fibroblasts, sDMA-containing proteins concentrated in speckles. Cells from a patient with spinal muscular atrophy, containing low levels of the methyl-binding protein SMN, localized sDMA-containing proteins in the nucleoplasm as a discrete granular pattern. Splicing reactions are efficiently inhibited by using the sDMA-specific antibody or by using hypomethylated nuclear extracts, showing that active spliceosomes contain sDMA polypeptides and suggesting that arginine methylation is important for efficient pre-mRNA splicing. Our findings support a model in which arginine methylation is important for the localization of coilin and SMN in Cajal bodies. The Rockefeller University Press 2002-12-23 /pmc/articles/PMC2173973/ /pubmed/12486110 http://dx.doi.org/10.1083/jcb.200207028 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Boisvert, François-Michel Côté, Jocelyn Boulanger, Marie-Chloé Cléroux, Patrick Bachand, François Autexier, Chantal Richard, Stéphane Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title | Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title_full | Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title_fullStr | Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title_full_unstemmed | Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title_short | Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing |
title_sort | symmetrical dimethylarginine methylation is required for the localization of smn in cajal bodies and pre-mrna splicing |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173973/ https://www.ncbi.nlm.nih.gov/pubmed/12486110 http://dx.doi.org/10.1083/jcb.200207028 |
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