The Library
BTB-BACK domain protein POB1 suppresses immune cell death by targeting ubiquitin E3 ligase PUB17 for degradation
Tools
Tools
Tools
Orosa, Beatriz, He, Qin, Mesmar, Joelle, Gilroy, Eleanor M., McLellan, Hazel, Yang, Chengwei, Craig, Adam, Bailey, Mark, Zhang, Cunjin, Moore, Jonathan D., Boevink, Petra C., Tian, Zhendong, Birch, Paul R. J. and Sadanandom, Ari (2017) BTB-BACK domain protein POB1 suppresses immune cell death by targeting ubiquitin E3 ligase PUB17 for degradation. PLoS Genetics, 13 (1). e1006540. doi:10.1371/journal.pgen.1006540 ISSN 1553-7390.
|
PDF
WRAP-BTB-BACK-domain-Moore-2017.pdf - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (2422Kb) | Preview |
Official URL: http://dx.doi.org/10.1371/journal.pgen.1006540
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.
| Item Type: | Journal Article | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | ?? Biology and life sciences ?? ?? Physical sciences ?? Q Science > QK Botany ?? Research Article ?? |
|||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Research Centres > Warwick Systems Biology Centre | |||||||||||||||
| SWORD Depositor: | Library Publications Router | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Plant immunology, Cell death, Plants -- Disease and pest resistance -- Molecular aspects, Ligases, Plant-pathogen relationships -- Molecular aspects, Apoptosis, Ubiquitin | |||||||||||||||
| Journal or Publication Title: | PLoS Genetics | |||||||||||||||
| Publisher: | Public Library of Science | |||||||||||||||
| ISSN: | 1553-7390 | |||||||||||||||
| Official Date: | 5 January 2017 | |||||||||||||||
| Dates: |
|
|||||||||||||||
| Volume: | 13 | |||||||||||||||
| Number: | 1 | |||||||||||||||
| Number of Pages: | 26 | |||||||||||||||
| Article Number: | e1006540 | |||||||||||||||
| DOI: | 10.1371/journal.pgen.1006540 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | |||||||||||||||
| RIOXX Funder/Project Grant: |
|
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
