NDLI: 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

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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

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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

Content Provider	PubMed Central
Author	Bailey, Mark Srivastava, Anjil Conti, Lucio Nelis, Stuart Zhang, Cunjin Florance, Hannah Love, Andrew Milner, Joel Napier, Richard Grant, Murray Ari, Sadanandom
Copyright Year	2015
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.
Related Links	http://dx.doi.org/10.1093/jxb/erv468
Ending Page	363
Page Count	11
Starting Page	353
File Format	PDF
ISSN	00220957
e-ISSN	14602431
Journal	Journal of Experimental Botany
Issue Number	1
Volume Number	67
Language	English
Publisher	Oxford University Press
Publisher Date	2016-01-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Plant Science Physiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Physiology Plant Science

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