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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2017
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.
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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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