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231224s2016 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erv468
|2 doi
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|a pubmed24n0846.xml
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|a (DE-627)NLM253951518
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|a (NLM)26494731
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Bailey, Mark
|e verfasserin
|4 aut
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|a 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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|c 2016
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 23.09.2016
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|a Date Revised 29.01.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arabidopsis thaliana
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|a SUMO protease
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|a SUMOylation.
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|a defence
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|a pathogen
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|a salicylic acid (SA)
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|a small ubiquitin-like modifier (SUMO)
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|a Arabidopsis Proteins
|2 NLM
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|a SUM1 protein, Arabidopsis
|2 NLM
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|a SUM2 protein, Arabidopsis
|2 NLM
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|a Cysteine Endopeptidases
|2 NLM
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|a EC 3.4.22.-
|2 NLM
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|a OTS1 protein, Arabidopsis
|2 NLM
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|a EC 3.4.22.-
|2 NLM
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|a OTS2 protein, Arabidopsis
|2 NLM
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|a EC 3.4.22.-
|2 NLM
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|a Salicylic Acid
|2 NLM
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|a O414PZ4LPZ
|2 NLM
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|a Srivastava, Anjil
|e verfasserin
|4 aut
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|a Conti, Lucio
|e verfasserin
|4 aut
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|a Nelis, Stuart
|e verfasserin
|4 aut
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|a Zhang, Cunjin
|e verfasserin
|4 aut
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|a Florance, Hannah
|e verfasserin
|4 aut
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|a Love, Andrew
|e verfasserin
|4 aut
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|a Milner, Joel
|e verfasserin
|4 aut
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|a Napier, Richard
|e verfasserin
|4 aut
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|a Grant, Murray
|e verfasserin
|4 aut
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|a Sadanandom, Ari
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 67(2016), 1 vom: 22. Jan., Seite 353-63
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:67
|g year:2016
|g number:1
|g day:22
|g month:01
|g pages:353-63
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|u http://dx.doi.org/10.1093/jxb/erv468
|3 Volltext
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|d 67
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|h 353-63
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