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

Sci Rep. 2018; 
Milić D,, Dick M,, Mulnaes D, Pfleger C, Kinnen A, Gohlke H,, Groth G.
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Peptide Synthesis C-terminally amidated peptides NOP-1 (LKRYKRRL-NH2), NIP-1 (AFPKGKENLASV LKRYKRRL-NH2), N30P (GRTGTAAGDVAFPKGKENLASVLKRYKRRL-NH2) and N41P (KDVEMAISSRKGRT GTAAGDVAFPKGKENLASVLKRYKRRL-NH2) were purchased from GenScript as lyophilized trifluoacetate (TFA) salts with > 98% HPLC purity and stored at −20 °C. Get A Quote

摘要

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.

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