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Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator.
David Latrasse, Teddy Jégu, Pin-Hong Meng, Christelle Mazubert, Elodie Hudik, Marianne Delarue, Céline Charon, Martin Crespi, Heribert Hirt, Cécile Raynaud, Catherine Bergounioux, Moussa Benhamed

Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator.

Science & Mathematics Published 2013 Verification Pending

Overview & Synopsis

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.

Indexed from repository: HAL Open Science (hal.science)
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Document Information

Document Title Dual function of MIPS1 as a metabolic enzyme and transcriptional regulator.
Author / Organization David Latrasse, Teddy Jégu, Pin-Hong Meng, Christelle Mazubert, Elodie Hudik, Marianne Delarue, Céline Charon, Martin Crespi, Heribert Hirt, Cécile Raynaud, Catherine Bergounioux, Moussa Benhamed
Subject & Discipline Multidisciplinary Academic Open Research
Categories Science & Mathematics
Publication Year 2013
License / Rights Open Access / Creative Commons
Resource Verification Listed PDF (Verification Pending)
Original Host Website HAL Open Science (hal.science)
File Format application/pdf (Portable Document Format)
Language EN
Catalog ID DOC-53888
Original Source Link Visit Source Page on hal.science »