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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...

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Autores principales: Boisvert, François-Michel, Côté, Jocelyn, Boulanger, Marie-Chloé, Cléroux, Patrick, Bachand, François, Autexier, Chantal, Richard, Stéphane
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2002
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.
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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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