Back to Search
Start Over
Protein lysine methylation is involved in modulating the response of sensitive and tolerant Arabidopsis species to cadmium stress
- Publication Year :
- 2019
- Publisher :
- Cold Spring Harbor Laboratory, 2019.
-
Abstract
- The mechanisms underlying the response and adaptation of plants to excess of trace elements are not fully described. Here, we analyzed the importance of protein lysine methylation for plants to cope with cadmium. We analyzed the effect of cadmium on lysine-methylated proteins and protein lysine methyltransferases (KMTs) in two cadmium-sensitive species,Arabidopsis thalianaandA. lyrata, and in three populations ofA. halleriwith contrasting cadmium accumulation and tolerance traits. We showed that some proteins are differentially methylated at lysine residues in response to Cd and that a few genes coding KMTs is regulated by cadmium. Also, we showed that nine out of 23A. thalianamutants interrupted inKMTgenes have a tolerance to cadmium that is significantly different from that of wild-type seedlings. We further characterized two of these mutants, one was knocked-out in the calmodulin lysine methyltransferase gene and displayed increased tolerance to cadmium, the other was interrupted in aKMTgene of unknown function and showed a decreased capacity to cope with cadmium. Together, our results showed that lysine methylation of non-histone proteins is impacted by cadmium and that several methylation events are important for modulating the response of Arabidopsis plants to cadmium stress.
- Subjects :
- 0106 biological sciences
inorganic chemicals
0303 health sciences
Cadmium
Methyltransferase
biology
Chemistry
Mutant
Lysine
chemistry.chemical_element
Methylation
biology.organism_classification
01 natural sciences
complex mixtures
03 medical and health sciences
Biochemistry
Arabidopsis
Arabidopsis thaliana
bacteria
Gene
030304 developmental biology
010606 plant biology & botany
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....f5b231764d463311f59344472221d2ca
- Full Text :
- https://doi.org/10.1101/652651