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<scp>UBC</scp> 18 mediates <scp>ERF</scp> 1 degradation under light–dark cycles
- Source :
- New Phytologist. 213:1156-1167
- Publication Year :
- 2016
- Publisher :
- Wiley, 2016.
-
Abstract
- Summary Ethylene Response Factor 1 (ERF1) plays a crucial role in biotic and abiotic stress responses. Previous studies have shown that ERF1 regulates stress-responsive gene expression by binding to different cis-acting elements in response to various stress signals. ERF1 was also reported to be unstable in the dark, and it regulates hypocotyl elongation. Here, we elucidated the mechanism underlying degradation of ERF1. Yeast two-hybrid screening showed that UBIQUITIN-CONJUGATING ENZYME 18 (UBC18) interacted with ERF1. The interaction between ERF1 and UBC18 was verified using pull-down assays and coimmunoprecipitation analyses. We then compared the ERF1 protein abundance in the UBC18 mutant and overexpression plants. Based on the results of protein degradation and in vivo ubiquitination assays, we proposed that UBC18 mediates ERF1 ubiquitination and degradation. ERF1 was more stable in UBC18 mutants and less stable in UBC18 overexpression lines compared with that in wild-type plants. ERF1 was degraded by the 26S proteasome system via regulation of UBC18 and promotes dark-repression of downstream genes and proline accumulation. UBC18 negatively regulated drought and salt stress responses by altering the abundance of ERF1 and the expression of genes downstream of ERF1.
- Subjects :
- DNA, Bacterial
0106 biological sciences
0301 basic medicine
Proteasome Endopeptidase Complex
Proline
Physiology
Immunoprecipitation
Photoperiod
Mutant
Arabidopsis
Plant Science
Sodium Chloride
Protein degradation
01 natural sciences
03 medical and health sciences
Ubiquitin
Gene Expression Regulation, Plant
Stress, Physiological
Gene expression
Gene
biology
Arabidopsis Proteins
Abiotic stress
Homozygote
Ubiquitination
Droughts
Cell biology
Phenotype
030104 developmental biology
Proteasome
Biochemistry
Proteolysis
Ubiquitin-Conjugating Enzymes
biology.protein
Peptide Termination Factors
Protein Binding
010606 plant biology & botany
Subjects
Details
- ISSN :
- 14698137 and 0028646X
- Volume :
- 213
- Database :
- OpenAIRE
- Journal :
- New Phytologist
- Accession number :
- edsair.doi.dedup.....baf46bc2398da6195805b1e13f3e8c62