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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Main Authors: Sebastian J. Nintemann, Daniel Vik, Julia Svozil, Michael Bak, Katja Baerenfaller, Meike Burow, Barbara A. Halkier
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-11-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fpls.2017.02028/full
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spelling doaj-76e9ea09f4dd41b387b21e6905de12b92020-11-25T00:04:03ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2017-11-01810.3389/fpls.2017.02028312095Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in ArabidopsisSebastian J. Nintemann0Daniel Vik1Julia Svozil2Michael Bak3Katja Baerenfaller4Meike Burow5Barbara A. Halkier6Department of Plant and Environmental Sciences, Faculty of Science, DynaMo Center, University of Copenhagen, Frederiksberg, DenmarkDepartment of Plant and Environmental Sciences, Faculty of Science, DynaMo Center, University of Copenhagen, Frederiksberg, DenmarkDepartment of Biology, ETH Zurich, Zurich, SwitzerlandDepartment of Plant and Environmental Sciences, Faculty of Science, DynaMo Center, University of Copenhagen, Frederiksberg, DenmarkDepartment of Biology, ETH Zurich, Zurich, SwitzerlandDepartment of Plant and Environmental Sciences, Faculty of Science, DynaMo Center, University of Copenhagen, Frederiksberg, DenmarkDepartment of Plant and Environmental Sciences, Faculty of Science, DynaMo Center, University of Copenhagen, Frederiksberg, DenmarkWithin 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.http://journal.frontiersin.org/article/10.3389/fpls.2017.02028/fullArabidopsis thalianaprotein-protein interactionsglucosinolatesregulatory networkspathway organization
collection DOAJ
language English
format Article
sources DOAJ
author Sebastian J. Nintemann
Daniel Vik
Julia Svozil
Michael Bak
Katja Baerenfaller
Meike Burow
Barbara A. Halkier
spellingShingle Sebastian J. Nintemann
Daniel Vik
Julia Svozil
Michael Bak
Katja Baerenfaller
Meike Burow
Barbara A. Halkier
Unravelling Protein-Protein Interaction Networks Linked to Aliphatic and Indole Glucosinolate Biosynthetic Pathways in Arabidopsis
Frontiers in Plant Science
Arabidopsis thaliana
protein-protein interactions
glucosinolates
regulatory networks
pathway organization
author_facet Sebastian J. Nintemann
Daniel Vik
Julia Svozil
Michael Bak
Katja Baerenfaller
Meike Burow
Barbara A. Halkier
author_sort Sebastian J. Nintemann
title 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_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_sort unravelling protein-protein interaction networks linked to aliphatic and indole glucosinolate biosynthetic pathways in arabidopsis
publisher Frontiers Media S.A.
series Frontiers in Plant Science
issn 1664-462X
publishDate 2017-11-01
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.
topic Arabidopsis thaliana
protein-protein interactions
glucosinolates
regulatory networks
pathway organization
url http://journal.frontiersin.org/article/10.3389/fpls.2017.02028/full
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