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Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator
Because regulation of its activity is instrumental either to support cell proliferation and growth or to promote cell death, the universal myo-inositol phosphate synthase (MIPS), responsible for myo-inositol biosynthesis, is a critical enzyme of primary metabolism. Surprisingly, we found this enzyme...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597657/ https://www.ncbi.nlm.nih.gov/pubmed/23341037 http://dx.doi.org/10.1093/nar/gks1458 |
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author | Latrasse, David Jégu, Teddy Meng, Pin-Hong Mazubert, Christelle Hudik, Elodie Delarue, Marianne Charon, Céline Crespi, Martin Hirt, Heribert Raynaud, Cécile Bergounioux, Catherine Benhamed, Moussa |
author_facet | Latrasse, David Jégu, Teddy Meng, Pin-Hong Mazubert, Christelle Hudik, Elodie Delarue, Marianne Charon, Céline Crespi, Martin Hirt, Heribert Raynaud, Cécile Bergounioux, Catherine Benhamed, Moussa |
author_sort | Latrasse, David |
collection | PubMed |
description | Because regulation of its activity is instrumental either to support cell proliferation and growth or to promote cell death, the universal myo-inositol phosphate synthase (MIPS), responsible for myo-inositol biosynthesis, is a critical enzyme of primary metabolism. Surprisingly, we found this enzyme to be imported in the nucleus and to interact with the histone methyltransferases ATXR5 and ATXR6, raising the question of whether MIPS1 has a function in transcriptional regulation. Here, we demonstrate that MIPS1 binds directly to its promoter to stimulate its own expression by locally inhibiting the spreading of ATXR5/6-dependent heterochromatin marks coming from a transposable element. Furthermore, on activation of pathogen response, MIPS1 expression is reduced epigenetically, providing evidence for a complex regulatory mechanism acting at the transcriptional level. Thus, in plants, MIPS1 appears to have evolved as a protein that connects cellular metabolism, pathogen response and chromatin remodeling. |
format | Online Article Text |
id | pubmed-3597657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-35976572013-03-15 Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator Latrasse, David Jégu, Teddy Meng, Pin-Hong Mazubert, Christelle Hudik, Elodie Delarue, Marianne Charon, Céline Crespi, Martin Hirt, Heribert Raynaud, Cécile Bergounioux, Catherine Benhamed, Moussa Nucleic Acids Res Gene Regulation, Chromatin and Epigenetics Because regulation of its activity is instrumental either to support cell proliferation and growth or to promote cell death, the universal myo-inositol phosphate synthase (MIPS), responsible for myo-inositol biosynthesis, is a critical enzyme of primary metabolism. Surprisingly, we found this enzyme to be imported in the nucleus and to interact with the histone methyltransferases ATXR5 and ATXR6, raising the question of whether MIPS1 has a function in transcriptional regulation. Here, we demonstrate that MIPS1 binds directly to its promoter to stimulate its own expression by locally inhibiting the spreading of ATXR5/6-dependent heterochromatin marks coming from a transposable element. Furthermore, on activation of pathogen response, MIPS1 expression is reduced epigenetically, providing evidence for a complex regulatory mechanism acting at the transcriptional level. Thus, in plants, MIPS1 appears to have evolved as a protein that connects cellular metabolism, pathogen response and chromatin remodeling. Oxford University Press 2013-03 2013-01-21 /pmc/articles/PMC3597657/ /pubmed/23341037 http://dx.doi.org/10.1093/nar/gks1458 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Gene Regulation, Chromatin and Epigenetics Latrasse, David Jégu, Teddy Meng, Pin-Hong Mazubert, Christelle Hudik, Elodie Delarue, Marianne Charon, Céline Crespi, Martin Hirt, Heribert Raynaud, Cécile Bergounioux, Catherine Benhamed, Moussa Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title | Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title_full | Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title_fullStr | Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title_full_unstemmed | Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title_short | Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator |
title_sort | dual function of mips1 as a metabolic enzyme and transcriptional regulator |
topic | Gene Regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3597657/ https://www.ncbi.nlm.nih.gov/pubmed/23341037 http://dx.doi.org/10.1093/nar/gks1458 |
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