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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2017
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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. |
format | Online Article Text |
id | pubmed-5712850 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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