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231226s2022 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2022.111357
|2 doi
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|a pubmed25n1141.xml
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|a (DE-627)NLM342396021
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|a (NLM)35718335
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|a (PII)S0168-9452(22)00181-9
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Zheng, Ting
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Arabidopsis SUMO E3 ligase SIZ1 enhances cadmium tolerance via the glutathione-dependent phytochelatin synthesis pathway
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|c 2022
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 21.07.2022
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|a Date Revised 21.07.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2022 Elsevier B.V. All rights reserved.
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|a Sumoylation is a posttranslational modification (PTM) in which SUMO (small ubiquitin-like modifier) is covalently conjugated to protein substrates via a range of enzymes. SUMO E3 ligase SIZ1 is involved in mediating several essential or nonessential element-responsive SUMO conjugations in Arabidopsis. However, whether SIZ1 is involved in the cadmium (Cd) response remains to be identified. In this study, we found that SIZ1 positively regulates plant Cd tolerance. The loss-of-function siz1-2 mutant exhibited impaired resistance to Cd exposure and accumulated more reactive oxygen species (ROS). Moreover, the transcription of GSH1, GSH2, PCS1, and PCS2 was suppressed while the accumulation of Cd was enhanced in the siz1-2 mutant under Cd exposure. Further analysis revealed that the higher Cd sensitivity of the siz1-2 mutant was partially rescued by the overexpression of GSH1. Consistently, Cd stress stimulated the accumulation of SUMO1 conjugates in wild-type plants but not in the siz1-2 mutant. Together, our results demonstrate that Cd-induced SIZ1 activates GSH- and PC synthesis-related gene expression to increase the synthesis of GSH- and PCs, thereby leading to higher Cd tolerance in plants
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|a Journal Article
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|a Cadmium
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|a Glutathione
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|a Phytochelatin
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|a SIZ1
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|a Sumoylation
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|a Arabidopsis Proteins
|2 NLM
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|a Cadmium
|2 NLM
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| 650 |
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|a 00BH33GNGH
|2 NLM
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|a Phytochelatins
|2 NLM
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| 650 |
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|a 98726-08-0
|2 NLM
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| 650 |
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|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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7 |
|a EC 2.3.2.27
|2 NLM
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| 650 |
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|a Ligases
|2 NLM
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| 650 |
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|a EC 6.-
|2 NLM
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| 650 |
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|a SIZ1 protein, Arabidopsis
|2 NLM
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| 650 |
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7 |
|a EC 6.3.2.-
|2 NLM
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| 650 |
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|a Glutamate-Cysteine Ligase
|2 NLM
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| 650 |
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7 |
|a EC 6.3.2.2
|2 NLM
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| 650 |
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|a Gsh1 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 6.3.2.2
|2 NLM
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| 650 |
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|a Glutathione
|2 NLM
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| 650 |
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|a GAN16C9B8O
|2 NLM
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| 700 |
1 |
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|a Wu, Guo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Tao, Xiang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a He, Bing
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 322(2022) vom: 01. Sept., Seite 111357
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnas
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| 773 |
1 |
8 |
|g volume:322
|g year:2022
|g day:01
|g month:09
|g pages:111357
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| 856 |
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|u http://dx.doi.org/10.1016/j.plantsci.2022.111357
|3 Volltext
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|d 322
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