Beatriz Orosa
BTB-BACK Domain Protein POB1 Suppresses Immune Cell Death by Targeting Ubiquitin E3 ligase PUB17 for Degradation
Orosa, Beatriz; He, Qin; Mesmar, Joelle; Gilroy, Eleanor M.; McLellan, Hazel; Yang, Chengwei; Craig, Adam; Bailey, Mark; Zhang, Cunjin; Moore, Jonathan David; Boevink, Petra C.; Tian, Zhendong; Birch, Paul R.J.; Sadanandom, Ari
Authors
Qin He
Joelle Mesmar
Eleanor M. Gilroy
Hazel McLellan
Chengwei Yang
Adam Craig
Mark Bailey
Dr Cunjin Zhang cunjin.zhang@durham.ac.uk
Senior Experimental Officer
Jonathan David Moore
Petra C. Boevink
Zhendong Tian
Paul R.J. Birch
Professor Ari Sadanandom ari.sadanandom@durham.ac.uk
Professor
Abstract
Hypersensitive response programmed cell death (HR-PCD) is a critical feature in plant immunity required for pathogen restriction and prevention of disease development. The precise control of this process is paramount to cell survival and an effective immune response. The discovery of new components that function to suppress HR-PCD will be instrumental in understanding the regulation of this fundamental mechanism. Here we report the identification and characterisation of a BTB domain E3 ligase protein, POB1, that functions to suppress HR-PCD triggered by evolutionarily diverse pathogens. Nicotiana benthamiana and tobacco plants with reduced POB1 activity show accelerated HR-PCD whilst those with increased POB1 levels show attenuated HR-PCD. We demonstrate that POB1 dimerization and nuclear localization are vital for its function in HR-PCD suppression. Using protein-protein interaction assays, we identify the Plant U-Box E3 ligase PUB17, a well established positive regulator of plant innate immunity, as a target for POB1-mediated proteasomal degradation. Using confocal imaging and in planta immunoprecipitation assays we show that POB1 interacts with PUB17 in the nucleus and stimulates its degradation. Mutated versions of POB1 that show reduced interaction with PUB17 fail to suppress HR-PCD, indicating that POB1-mediated degradation of PUB17 U-box E3 ligase is an important step for negative regulation of specific immune pathways in plants. Our data reveals a new mechanism for BTB domain proteins in suppressing HR-PCD in plant innate immune responses.
Citation
Orosa, B., He, Q., Mesmar, J., Gilroy, E. M., McLellan, H., Yang, C., …Sadanandom, A. (2017). BTB-BACK Domain Protein POB1 Suppresses Immune Cell Death by Targeting Ubiquitin E3 ligase PUB17 for Degradation. PLoS Genetics, 13(1), Article e1006540. https://doi.org/10.1371/journal.pgen.1006540
Journal Article Type | Article |
---|---|
Acceptance Date | Dec 15, 2016 |
Online Publication Date | Jan 5, 2017 |
Publication Date | Jan 5, 2017 |
Deposit Date | Jul 25, 2017 |
Publicly Available Date | Jul 25, 2017 |
Journal | PLoS Genetics |
Print ISSN | 1553-7390 |
Electronic ISSN | 1553-7404 |
Publisher | Public Library of Science |
Peer Reviewed | Peer Reviewed |
Volume | 13 |
Issue | 1 |
Article Number | e1006540 |
DOI | https://doi.org/10.1371/journal.pgen.1006540 |
Public URL | https://durham-repository.worktribe.com/output/1351316 |
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Copyright Statement
© 2017 Orosa et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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