Journal
JOURNAL OF EXPERIMENTAL BOTANY
Volume 67, Issue 1, Pages 353-363Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jxb/erv468
Keywords
Arabidopsis thaliana; defence; pathogen; salicylic acid (SA); small ubiquitin-like modifier (SUMO); SUMO protease; SUMOylation
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Funding
- Biological and Biotechnological Research Council
- European Research Council (ERC)
- BBSRC [BB/D017319]
- BBSRC [BB/D017319/1, BB/D007046/1, BB/M002136/1, BB/F005903/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L009366/1, BB/D017319/1, BB/M002136/1, BB/F005903/1, BB/D007046/1] Funding Source: researchfish
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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.
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