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Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
Biochemical purifications from mammalian cells and Xenopus oocytes revealed that vertebrate Mi-2 proteins reside in multisubunit NuRD (Nucleosome Remodeling and Deacetylase) complexes. Since all NuRD subunits are highly conserved in the genomes of C. elegans and Drosophila, it was suggested that NuR...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2965115/ https://www.ncbi.nlm.nih.gov/pubmed/21060680 http://dx.doi.org/10.1371/journal.pone.0013681 |
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author | Passannante, Myriam Marti, Claude-Olivier Pfefferli, Catherine Moroni, Paolo S. Kaeser-Pebernard, Stéphanie Puoti, Alessandro Hunziker, Peter Wicky, Chantal Müller, Fritz |
author_facet | Passannante, Myriam Marti, Claude-Olivier Pfefferli, Catherine Moroni, Paolo S. Kaeser-Pebernard, Stéphanie Puoti, Alessandro Hunziker, Peter Wicky, Chantal Müller, Fritz |
author_sort | Passannante, Myriam |
collection | PubMed |
description | Biochemical purifications from mammalian cells and Xenopus oocytes revealed that vertebrate Mi-2 proteins reside in multisubunit NuRD (Nucleosome Remodeling and Deacetylase) complexes. Since all NuRD subunits are highly conserved in the genomes of C. elegans and Drosophila, it was suggested that NuRD complexes also exist in invertebrates. Recently, a novel dMec complex, composed of dMi-2 and dMEP-1 was identified in Drosophila. The genome of C. elegans encodes two highly homologous Mi-2 orthologues, LET-418 and CHD-3. Here we demonstrate that these proteins define at least three different protein complexes, two distinct NuRD complexes and one MEC complex. The two canonical NuRD complexes share the same core subunits HDA-1/HDAC, LIN-53/RbAp and LIN-40/MTA, but differ in their Mi-2 orthologues LET-418 or CHD-3. LET-418 but not CHD-3, interacts with the Krüppel-like protein MEP-1 in a distinct complex, the MEC complex. Based on microarrays analyses, we propose that MEC constitutes an important LET-418 containing regulatory complex during C. elegans embryonic and early larval development. It is required for the repression of germline potential in somatic cells and acts when blastomeres are still dividing and differentiating. The two NuRD complexes may not be important for the early development, but may act later during postembryonic development. Altogether, our data suggest a considerable complexity in the composition, the developmental function and the tissue-specificity of the different C. elegans Mi-2 complexes. |
format | Text |
id | pubmed-2965115 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29651152010-11-08 Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans Passannante, Myriam Marti, Claude-Olivier Pfefferli, Catherine Moroni, Paolo S. Kaeser-Pebernard, Stéphanie Puoti, Alessandro Hunziker, Peter Wicky, Chantal Müller, Fritz PLoS One Research Article Biochemical purifications from mammalian cells and Xenopus oocytes revealed that vertebrate Mi-2 proteins reside in multisubunit NuRD (Nucleosome Remodeling and Deacetylase) complexes. Since all NuRD subunits are highly conserved in the genomes of C. elegans and Drosophila, it was suggested that NuRD complexes also exist in invertebrates. Recently, a novel dMec complex, composed of dMi-2 and dMEP-1 was identified in Drosophila. The genome of C. elegans encodes two highly homologous Mi-2 orthologues, LET-418 and CHD-3. Here we demonstrate that these proteins define at least three different protein complexes, two distinct NuRD complexes and one MEC complex. The two canonical NuRD complexes share the same core subunits HDA-1/HDAC, LIN-53/RbAp and LIN-40/MTA, but differ in their Mi-2 orthologues LET-418 or CHD-3. LET-418 but not CHD-3, interacts with the Krüppel-like protein MEP-1 in a distinct complex, the MEC complex. Based on microarrays analyses, we propose that MEC constitutes an important LET-418 containing regulatory complex during C. elegans embryonic and early larval development. It is required for the repression of germline potential in somatic cells and acts when blastomeres are still dividing and differentiating. The two NuRD complexes may not be important for the early development, but may act later during postembryonic development. Altogether, our data suggest a considerable complexity in the composition, the developmental function and the tissue-specificity of the different C. elegans Mi-2 complexes. Public Library of Science 2010-10-27 /pmc/articles/PMC2965115/ /pubmed/21060680 http://dx.doi.org/10.1371/journal.pone.0013681 Text en Passannante et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Passannante, Myriam Marti, Claude-Olivier Pfefferli, Catherine Moroni, Paolo S. Kaeser-Pebernard, Stéphanie Puoti, Alessandro Hunziker, Peter Wicky, Chantal Müller, Fritz Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans |
title | Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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title_full | Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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title_fullStr | Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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title_full_unstemmed | Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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title_short | Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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title_sort | different mi-2 complexes for various developmental functions in caenorhabditis elegans |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2965115/ https://www.ncbi.nlm.nih.gov/pubmed/21060680 http://dx.doi.org/10.1371/journal.pone.0013681 |
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