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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...

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Autores principales: Passannante, Myriam, Marti, Claude-Olivier, Pfefferli, Catherine, Moroni, Paolo S., Kaeser-Pebernard, Stéphanie, Puoti, Alessandro, Hunziker, Peter, Wicky, Chantal, Müller, Fritz
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
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.
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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
title_full Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
title_fullStr Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
title_full_unstemmed Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
title_short Different Mi-2 Complexes for Various Developmental Functions in Caenorhabditis elegans
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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