Recognition motif and mechanism of ripening inhibitory peptides in plant hormone receptor ETR1

 

Li X, Hao G, Wang Q, Chen Z, Ding Y, Yu L, Hu D, Song B.

Scientific Reports
2018 Mar 1;8(1):3890. doi: 10.1038/s41598-018-21952-3

Abstract

Synthetic peptides derived from ethylene-insensitive protein 2 (EIN2), a central regulator of ethylene signalling, were recently shown to delay fruit ripening by interrupting protein-protein interactions in the ethylene signalling pathway. Here, we show that the inhibitory peptide NOP-1 binds to the GAF domain of ETR1 - the prototype of the plant ethylene receptor family. Site-directed mutagenesis and computational studies reveal the peptide interaction site and a plausible molecular mechanism for the ripening inhibition.

View Publication

Topics: Plant proteins, Monolith – MicroScale Thermophoresis, MST, Proteins, Publications

 

 

Previous Article
Trehalose 6-phosphate positively regulates fatty acid synthesis by stabilizing WRINKLED1
Trehalose 6-phosphate positively regulates fatty acid synthesis by stabilizing WRINKLED1

Up next
The ACT domain in chloroplast precursor–phosphorylating STY kinases binds metabolites and allosterically regulates kinase activity
The ACT domain in chloroplast precursor–phosphorylating STY kinases binds metabolites and allosterically regulates kinase activity