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

© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 67(2016), 1 vom: 22. Jan., Seite 353-63
1. Verfasser: Bailey, Mark (VerfasserIn)
Weitere Verfasser: Srivastava, Anjil, Conti, Lucio, Nelis, Stuart, Zhang, Cunjin, Florance, Hannah, Love, Andrew, Milner, Joel, Napier, Richard, Grant, Murray, Sadanandom, Ari
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana SUMO protease SUMOylation. defence pathogen salicylic acid (SA) small ubiquitin-like modifier (SUMO) Arabidopsis Proteins mehr... SUM1 protein, Arabidopsis SUM2 protein, Arabidopsis Cysteine Endopeptidases EC 3.4.22.- OTS1 protein, Arabidopsis OTS2 protein, Arabidopsis Salicylic Acid O414PZ4LPZ
Beschreibung
Zusammenfassung:© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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
Beschreibung:Date Completed 23.09.2016
Date Revised 29.01.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erv468