Mark Bailey
Stability of small ubiquitin-like modifier (SUMO) proteases OVERLY TOLERANT TO SALT1 and -2 modulates salicylic acid signalling and SUMO1/2 conjugation in Arabidopsis thaliana
Bailey, Mark; Srivastava, Anjil; Conti, Lucio; Nelis, Stuart; Zhang, Cunjin; Florance, Hannah; Love, Andrew; Milner, Joel; Napier, Richard; Grant, Murray; Sadanandom, Ari
Authors
Anjil Srivastava
Lucio Conti
Stuart Nelis
Cunjin Zhang
Hannah Florance
Andrew Love
Joel Milner
Richard Napier
Murray Grant
Professor Ari Sadanandom ari.sadanandom@durham.ac.uk
Professor
Abstract
Small ubiquitin-like modifier proteases 1 and 2 (SUMO1/2) have been linked to the regulation of salicylic acid (SA)-mediated defence signalling in Arabidopsis thaliana. In order to define the role of the SUMO proteases OVERLY TOLERANT TO SALT1 and -2 (OTS1/2) in defence and to provide insight into SUMO1/2-mediated regulation of SA signalling, we examined the status of SA-mediated defences in ots1/2 mutants. The ots1 ots2 double mutant displayed enhanced resistance to virulent Pseudomonas syringae and higher levels of SA compared with wild-type (WT) plants. Furthermore, ots1 ots2 mutants exhibited upregulated expression of the SA biosynthesis gene ICS1 in addition to enhanced SA-responsive ICS1 expression beyond that of WT. SA stimulated OTS1/2 degradation and promoted accumulation of SUMO1/2 conjugates. These results indicate that OTS1 and -2 act in a feedback loop in SA signalling and that de novo OTS1/2 synthesis works antagonistically to SA-promoted degradation, adjusting the abundance of OTS1/2 to moderate SA signalling. Accumulation of SUMO1/2 conjugates coincides with SA-promoted OTS degradation and may play a positive role in SA-mediated signalling in addition to its repressive roles reported elsewhere.
Citation
Bailey, M., Srivastava, A., Conti, L., Nelis, S., Zhang, C., Florance, H., …Sadanandom, A. (2016). Stability of small ubiquitin-like modifier (SUMO) proteases OVERLY TOLERANT TO SALT1 and -2 modulates salicylic acid signalling and SUMO1/2 conjugation in Arabidopsis thaliana. Journal of Experimental Botany, 67(1), 353-363. https://doi.org/10.1093/jxb/erv468
Journal Article Type | Article |
---|---|
Acceptance Date | Oct 5, 2015 |
Online Publication Date | Oct 22, 2015 |
Publication Date | Jan 1, 2016 |
Deposit Date | Nov 2, 2015 |
Publicly Available Date | Nov 3, 2015 |
Journal | Journal of Experimental Botany |
Print ISSN | 0022-0957 |
Electronic ISSN | 1460-2431 |
Publisher | Oxford University Press |
Peer Reviewed | Peer Reviewed |
Volume | 67 |
Issue | 1 |
Pages | 353-363 |
DOI | https://doi.org/10.1093/jxb/erv468 |
Keywords | Arabidopsis thaliana, Defence, Pathogen, Salicylic acid (SA), Small ubiquitin-like modifier (SUMO), SUMO protease, SUMOylation. |
Public URL | https://durham-repository.worktribe.com/output/1427568 |
Files
Published Journal Article (Final published version)
(3.6 Mb)
PDF
Publisher Licence URL
http://creativecommons.org/licenses/by/3.0/
Copyright Statement
Final published version
Published Journal Article (Advance online version)
(1.3 Mb)
PDF
Publisher Licence URL
http://creativecommons.org/licenses/by/3.0/
Copyright Statement
Advance online version © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
You might also like
Towards understanding the multifaceted role of SUMOylation in plant growth and development
(2020)
Journal Article
SUMO Suppresses the Activity of the Jasmonic Acid Receptor CORONATINE INSENSITIVE1
(2018)
Journal Article
Exploiting protein modification systems to boost crop productivity: SUMO proteases in focus
(2018)
Journal Article