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TitleSuccessive domain rearrangements underlie the evolution of a regulatory module controlled by a small interfering peptide
Author(s)Raimundo, João Alexandre Pereira
Sobral, Rómulo Sacramento
Laranjeira, Sara
Costa, Maria Manuela Ribeiro
Protein evolution
Protein-protein interaction
Domain earrangement
Molecular antagonism
Small interfering peptide
Flower asymmetry
Antirrhinum majus
Domain rearrangement
Issue date2018
PublisherOxford University Press
JournalMolecular Biology and Evolution
CitationRaimundo, J., Sobral, R., Laranjeira, S., & Costa, M. M. R. (2018). Successive domain rearrangements underlie the evolution of a regulatory module controlled by a small interfering peptide. Molecular biology and evolution, 35(12), 2873-2885
Abstract(s)The establishment of new interactions between transcriptional regulators increases the regulatory diversity that drives phenotypic novelty. To understand how such interactions evolve, we have studied a regulatory module (DDR) composed by three MYB-like proteins: DIVARICATA (DIV), RADIALIS (RAD), and DIV-and-RAD-Interacting Factor (DRIF). The DIV and DRIF proteins form a transcriptional complex that is disrupted in the presence of RAD, a small interfering peptide, due to the formation of RAD-DRIF dimers. This dynamic interaction result in a molecular switch mechanism responsible for the control of distinct developmental processes in plants. Here, we have determined how the DDR regulatory module was established by analyzing the origin and evolution of the DIV, DRIF, and RAD protein families and the evolutionary history of their interactions. We show that duplications of a pre-existing MYB domain originated the DIV and DRIF protein families in the ancestral lineage of green algae, and, later, the RAD family in seed plants. Intraspecies interactions between the MYB domains of DIV and DRIF proteins are detected in green algae, whereas the earliest evidence of an interaction between DRIF and RAD proteins occurs in the gymnosperms, coincident with the establishment of the RAD family. Therefore, the DDR module evolved in a stepwise progression with the DIV-DRIF transcription complex evolving prior to the antagonistic RAD-DRIF interaction that established the molecular switch mechanism. Our results suggest that the successive rearrangement and divergence of a single protein domain can be an effective evolutionary mechanism driving new protein interactions and the establishment of novel regulatory modules.
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