Abstract
Evolution often diversifies a peptide hormone family into multiple subfamilies, which exert distinct activities by exclusive interaction with specific receptors. Here we show that systematic swapping of pre-existing variation in a subfamily of plant CLE peptide hormones leads to a synthetic bifunctional peptide that exerts activities beyond the original subfamily by interacting with multiple receptors. This approach provides new insights into the complexity and specificity of peptide signalling.
Highlights
Evolution often diversifies a peptide hormone family into multiple subfamilies, which exert distinct activities by exclusive interaction with specific receptors
The CLE genes acting for the shoot and root meristems (CLV3 and CLE40, respectively) are functionally exchangeable as revealed by a promoter-swapping analysis[5,6] and chemically synthesized 12 amino-acid CLV3 acts on both tissues; its overdose diminishes the growth of shoot and root[3]
The size of the root apical meristem (RAM) was reduced in CLV3, CLE25- and KIN-treated plants, which was not observed in CLE41-treated plants (Fig. 1c)
Summary
Evolution often diversifies a peptide hormone family into multiple subfamilies, which exert distinct activities by exclusive interaction with specific receptors. We show that systematic swapping of pre-existing variation in a subfamily of plant CLE peptide hormones leads to a synthetic bifunctional peptide that exerts activities beyond the original subfamily by interacting with multiple receptors. This approach provides new insights into the complexity and specificity of peptide signalling. Among 32 genes in the Arabidopsis thaliana CLE family, different sets of members are expressed in the three types of stem cell tissues: shoot, root and vascular meristems, regulating the homeostasis of stem cell populations[4]. CLV1 and TDR are transmembrane receptors for CLV3 and CLE41/TDIF, respectively, and the difference between their bioactivities lies in the specificity in ligand-receptor interaction[7,9,10], the structural basis of the specificity has not been fully understood[11,12,13]
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