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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 and Srivastava, Anjil and Conti, Lucio and Nelis, Stuart and Zhang, Cunjin and Florance, Hannah and Love, Andrew and Milner, Joel and Napier, Richard and Grant, Murray and Sadanandom, Ari (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). pp. 353-363.

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.

Item Type:Article
Keywords:Arabidopsis thaliana, Defence, Pathogen, Salicylic acid (SA), Small ubiquitin-like modifier (SUMO), SUMO protease, SUMOylation.
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Full text:(VoR) Version of Record
Available under License - Creative Commons Attribution.
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Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.1093/jxb/erv468
Publisher statement:© 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.
Date accepted:05 October 2015
Date deposited:03 November 2015
Date of first online publication:22 October 2015
Date first made open access:No date available

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