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Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus

Plant flavonoid metabolism has served as a platform for understanding a range of fundamental biological phenomena, including providing some of the early insights into the subcellular organization of metabolism. Evidence assembled over the past three decades points to the organization of the componen...

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Autores principales: Watkinson, Jonathan I., Bowerman, Peter A., Crosby, Kevin C., Hildreth, Sherry B., Helm, Richard F., Winkel, Brenda S.J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151112/
https://www.ncbi.nlm.nih.gov/pubmed/30258711
http://dx.doi.org/10.7717/peerj.5598
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author Watkinson, Jonathan I.
Bowerman, Peter A.
Crosby, Kevin C.
Hildreth, Sherry B.
Helm, Richard F.
Winkel, Brenda S.J.
author_facet Watkinson, Jonathan I.
Bowerman, Peter A.
Crosby, Kevin C.
Hildreth, Sherry B.
Helm, Richard F.
Winkel, Brenda S.J.
author_sort Watkinson, Jonathan I.
collection PubMed
description Plant flavonoid metabolism has served as a platform for understanding a range of fundamental biological phenomena, including providing some of the early insights into the subcellular organization of metabolism. Evidence assembled over the past three decades points to the organization of the component enzymes as a membrane-associated complex centered on the entry-point enzyme, chalcone synthase (CHS), with flux into branch pathways controlled by competitive protein interactions. Flavonoid enzymes have also been found in the nucleus in a variety of plant species, raising the possibility of alternative, or moonlighting functions for these proteins in this compartment. Here, we present evidence that CHS interacts with MOS9, a nuclear-localized protein that has been linked to epigenetic control of R genes that mediate effector-triggered immunity. Overexpression of MOS9 results in a reduction of CHS transcript levels and a metabolite profile that substantially intersects with the effects of a null mutation in CHS. These results suggest that the MOS9–CHS interaction may point to a previously-unknown mechanism for controlling the expression of the highly dynamic flavonoid pathway.
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spelling pubmed-61511122018-09-26 Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus Watkinson, Jonathan I. Bowerman, Peter A. Crosby, Kevin C. Hildreth, Sherry B. Helm, Richard F. Winkel, Brenda S.J. PeerJ Biochemistry Plant flavonoid metabolism has served as a platform for understanding a range of fundamental biological phenomena, including providing some of the early insights into the subcellular organization of metabolism. Evidence assembled over the past three decades points to the organization of the component enzymes as a membrane-associated complex centered on the entry-point enzyme, chalcone synthase (CHS), with flux into branch pathways controlled by competitive protein interactions. Flavonoid enzymes have also been found in the nucleus in a variety of plant species, raising the possibility of alternative, or moonlighting functions for these proteins in this compartment. Here, we present evidence that CHS interacts with MOS9, a nuclear-localized protein that has been linked to epigenetic control of R genes that mediate effector-triggered immunity. Overexpression of MOS9 results in a reduction of CHS transcript levels and a metabolite profile that substantially intersects with the effects of a null mutation in CHS. These results suggest that the MOS9–CHS interaction may point to a previously-unknown mechanism for controlling the expression of the highly dynamic flavonoid pathway. PeerJ Inc. 2018-09-19 /pmc/articles/PMC6151112/ /pubmed/30258711 http://dx.doi.org/10.7717/peerj.5598 Text en © 2018 Watkinson 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 Biochemistry
Watkinson, Jonathan I.
Bowerman, Peter A.
Crosby, Kevin C.
Hildreth, Sherry B.
Helm, Richard F.
Winkel, Brenda S.J.
Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title_full Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title_fullStr Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title_full_unstemmed Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title_short Identification of MOS9 as an interaction partner for chalcone synthase in the nucleus
title_sort identification of mos9 as an interaction partner for chalcone synthase in the nucleus
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6151112/
https://www.ncbi.nlm.nih.gov/pubmed/30258711
http://dx.doi.org/10.7717/peerj.5598
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