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The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development
The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polym...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5464003/ https://www.ncbi.nlm.nih.gov/pubmed/28603670 http://dx.doi.org/10.7717/peerj.3390 |
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author | Kostrouchová, Markéta Kostrouch, David Chughtai, Ahmed A. Kaššák, Filip Novotný, Jan P. Kostrouchová, Veronika Benda, Aleš Krause, Michael W. Saudek, Vladimír Kostrouchová, Marta Kostrouch, Zdeněk |
author_facet | Kostrouchová, Markéta Kostrouch, David Chughtai, Ahmed A. Kaššák, Filip Novotný, Jan P. Kostrouchová, Veronika Benda, Aleš Krause, Michael W. Saudek, Vladimír Kostrouchová, Marta Kostrouch, Zdeněk |
author_sort | Kostrouchová, Markéta |
collection | PubMed |
description | The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in Caenorhabditis elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other Metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. F28F8.5 interacts on the protein level with the Mediator subunits MDT-6 and MDT-30. Our results indicate that F28F8.5 is an orthologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode orthologues. |
format | Online Article Text |
id | pubmed-5464003 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54640032017-06-09 The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development Kostrouchová, Markéta Kostrouch, David Chughtai, Ahmed A. Kaššák, Filip Novotný, Jan P. Kostrouchová, Veronika Benda, Aleš Krause, Michael W. Saudek, Vladimír Kostrouchová, Marta Kostrouch, Zdeněk PeerJ Cell Biology The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in Caenorhabditis elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other Metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. F28F8.5 interacts on the protein level with the Mediator subunits MDT-6 and MDT-30. Our results indicate that F28F8.5 is an orthologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode orthologues. PeerJ Inc. 2017-06-06 /pmc/articles/PMC5464003/ /pubmed/28603670 http://dx.doi.org/10.7717/peerj.3390 Text en © 2017 Kostrouchová 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Cell Biology Kostrouchová, Markéta Kostrouch, David Chughtai, Ahmed A. Kaššák, Filip Novotný, Jan P. Kostrouchová, Veronika Benda, Aleš Krause, Michael W. Saudek, Vladimír Kostrouchová, Marta Kostrouch, Zdeněk The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title | The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title_full | The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title_fullStr | The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title_full_unstemmed | The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title_short | The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development |
title_sort | nematode homologue of mediator complex subunit 28, f28f8.5, is a critical regulator of c. elegans development |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5464003/ https://www.ncbi.nlm.nih.gov/pubmed/28603670 http://dx.doi.org/10.7717/peerj.3390 |
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