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Updated: May 10, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Evolutionary relationship and structural characterization of the EPF/EPFL gene family
Naoki Takata1, Kiyonobu Yokota, Shinya Ohki
1Forest Bio-Research Center, Forestry and Forest Products Research Institute, Hitachi, Japan.
Abstract:
EPF1-EPF2 and EPFL9/Stomagen act antagonistically in regulating leaf stomatal density. The aim of this study was to elucidate the evolutionary functional divergence of EPF/EPFL family genes. Phylogenetic analyses showed that AtEPFL9/Stomagen-like genes are conserved only in vascular plants and are closely related to AtEPF1/EPF2-like genes. Modeling showed that EPF/EPFL peptides share a common 3D structure that is constituted of a scaffold and loop. Molecular dynamics simulation suggested that AtEPF1/EPF2-like peptides form an additional disulfide bond in their loop regions and show greater flexibility in these regions than AtEPFL9/Stomagen-like peptides. This study uncovered the evolutionary relationship and the conformational divergence of proteins encoded by the EPF/EPFL family genes.
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The duplicated copies of the gene are called Paralogs. Paralogs with similar sequences and functions form a gene family. Across several species, a large number of gene families are characterized.

