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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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2017-11-01
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Series: | Frontiers in Plant Science |
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Online Access: | http://journal.frontiersin.org/article/10.3389/fpls.2017.02028/full |
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author | Sebastian J. Nintemann Daniel Vik Julia Svozil Michael Bak Katja Baerenfaller Meike Burow Barbara A. Halkier |
author_facet | Sebastian J. Nintemann Daniel Vik Julia Svozil Michael Bak Katja Baerenfaller Meike Burow Barbara A. Halkier |
author_sort | Sebastian J. Nintemann |
collection | DOAJ |
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. |
first_indexed | 2024-12-22T06:20:53Z |
format | Article |
id | doaj.art-76e9ea09f4dd41b387b21e6905de12b9 |
institution | Directory Open Access Journal |
issn | 1664-462X |
language | English |
last_indexed | 2024-12-22T06:20:53Z |
publishDate | 2017-11-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Plant Science |
spelling | doaj.art-76e9ea09f4dd41b387b21e6905de12b92022-12-21T18:35:58ZengFrontiers 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 |
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 |
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 | 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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