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Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis

Within the cell, biosynthetic pathways are embedded in protein-protein interaction networks. In Arabidopsis, the biosynthetic pathways of aliphatic and indole glucosinolate defense compounds are well-characterized. However, little is known about the spatial orchestration of these enzymes and their i...

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Autores principales: Nintemann, Sebastian J., Vik, Daniel, Svozil, Julia, Bak, Michael, Baerenfaller, Katja, Burow, Meike, Halkier, Barbara A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5712850/
https://www.ncbi.nlm.nih.gov/pubmed/29238354
http://dx.doi.org/10.3389/fpls.2017.02028
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author Nintemann, Sebastian J.
Vik, Daniel
Svozil, Julia
Bak, Michael
Baerenfaller, Katja
Burow, Meike
Halkier, Barbara A.
author_facet Nintemann, Sebastian J.
Vik, Daniel
Svozil, Julia
Bak, Michael
Baerenfaller, Katja
Burow, Meike
Halkier, Barbara A.
author_sort Nintemann, Sebastian J.
collection PubMed
description Within the cell, biosynthetic pathways are embedded in protein-protein interaction networks. In Arabidopsis, the biosynthetic pathways of aliphatic and indole glucosinolate defense compounds are well-characterized. However, little is known about the spatial orchestration of these enzymes and their interplay with the cellular environment. To address these aspects, we applied two complementary, untargeted approaches—split-ubiquitin yeast 2-hybrid and co-immunoprecipitation screens—to identify proteins interacting with CYP83A1 and CYP83B1, two homologous enzymes specific for aliphatic and indole glucosinolate biosynthesis, respectively. Our analyses reveal distinct functional networks with substantial interconnection among the identified interactors for both pathway-specific markers, and add to our knowledge about how biochemical pathways are connected to cellular processes. Specifically, a group of protein interactors involved in cell death and the hypersensitive response provides a potential link between the glucosinolate defense compounds and defense against biotrophic pathogens, mediated by protein-protein interactions.
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spelling pubmed-57128502017-12-13 Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis Nintemann, Sebastian J. Vik, Daniel Svozil, Julia Bak, Michael Baerenfaller, Katja Burow, Meike Halkier, Barbara A. Front Plant Sci Plant Science Within the cell, biosynthetic pathways are embedded in protein-protein interaction networks. In Arabidopsis, the biosynthetic pathways of aliphatic and indole glucosinolate defense compounds are well-characterized. However, little is known about the spatial orchestration of these enzymes and their interplay with the cellular environment. To address these aspects, we applied two complementary, untargeted approaches—split-ubiquitin yeast 2-hybrid and co-immunoprecipitation screens—to identify proteins interacting with CYP83A1 and CYP83B1, two homologous enzymes specific for aliphatic and indole glucosinolate biosynthesis, respectively. Our analyses reveal distinct functional networks with substantial interconnection among the identified interactors for both pathway-specific markers, and add to our knowledge about how biochemical pathways are connected to cellular processes. Specifically, a group of protein interactors involved in cell death and the hypersensitive response provides a potential link between the glucosinolate defense compounds and defense against biotrophic pathogens, mediated by protein-protein interactions. Frontiers Media S.A. 2017-11-29 /pmc/articles/PMC5712850/ /pubmed/29238354 http://dx.doi.org/10.3389/fpls.2017.02028 Text en Copyright © 2017 Nintemann, Vik, Svozil, Bak, Baerenfaller, Burow and Halkier. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Nintemann, Sebastian J.
Vik, Daniel
Svozil, Julia
Bak, Michael
Baerenfaller, Katja
Burow, Meike
Halkier, Barbara A.
Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title_full Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title_fullStr Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title_full_unstemmed Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title_short Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
title_sort unravelling protein-protein interaction networks linked to aliphatic and indole glucosinolate biosynthetic pathways in arabidopsis
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5712850/
https://www.ncbi.nlm.nih.gov/pubmed/29238354
http://dx.doi.org/10.3389/fpls.2017.02028
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