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Functional analysis of tomato CHIP ubiquitin E3 ligase in heat tolerance
- Source :
- Scientific Reports, Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
- Publication Year :
- 2021
- Publisher :
- Springer Science and Business Media LLC, 2021.
-
Abstract
- Plants have evolved genetic and physiological mechanisms to mitigate the adverse effects of high temperature. CARBOXYL TERMINUS OF THE HSC70-INTERACTING PROTEINS (CHIP) is a conserved chaperone-dependent ubiquitin E3 ligase that targets misfolded proteins. Here, we report functional analysis of the SlCHIP gene from tomato (Solanum lycopersicum) in heat tolerance. SlCHIP encodes a CHIP protein with three tandem tetracopeptide repeat (TPR) motifs and a C-terminal U box domain. Phylogenetic analysis of CHIP homologs from animals, spore-bearing and seed plants revealed a tree topology similar to the evolutionary tree of the organisms. Expression of SlCHIP was induced under high temperature and was also responsive to plant stress hormones. Silencing of SlCHIP in tomato reduced heat tolerance based on increased heat stress symptoms, reduced photosynthetic activity, elevated electrolyte leakage and accumulation of insoluble protein aggregates. The accumulated protein aggregates in SlCHIP-silenced plants were still highly ubiquitinated, suggesting involvement of other E3 ligases in ubiquitination. SlCHIP restored the heat tolerance of Arabidopsis chip mutant to the wild type levels. These results indicate that tomato SlCHIP plays a critical role in heat stress responses most likely by targeting degradation of misfolded proteins that are generated during heat stress.
- Subjects :
- Thermotolerance
0106 biological sciences
0301 basic medicine
Science
Ubiquitin-Protein Ligases
Mutant
Arabidopsis
Protein aggregation
01 natural sciences
Article
Protein Aggregates
03 medical and health sciences
Solanum lycopersicum
Protein Domains
Ubiquitin
Genetics
Animals
Amino Acid Sequence
Photosynthesis
Gene
Phylogeny
Plant Proteins
Multidisciplinary
biology
Chemistry
fungi
Temperature
Ubiquitination
Wild type
food and beverages
biology.organism_classification
Cell biology
Ubiquitin ligase
030104 developmental biology
Tandem Repeat Sequences
biology.protein
Medicine
RNA Interference
Protein folding
Plant sciences
Sequence Alignment
010606 plant biology & botany
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 11
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....90e27286ee36b895edc680b070145083
- Full Text :
- https://doi.org/10.1038/s41598-021-81372-8