Researchers at RIKEN and Keio University have shown that even the most widely-varying species of plants share remarkable similarities in the composition of proteins in them that undergo phosphorylation, a regulatory mechanism involved in various cellular phenomena. A database released by the group, with information on over three thousand phosphorylated proteins and phosphorylation sites in rice, opens new doors in the study and engineering of plants.
The addition of a phosphate group to a protein, known as phosphorylation, plays a vital role in regulating cellular phenomena and as a mediator of signaling pathways in the cell. The function of this process in regulating plant growth and development in particular makes it highly attractive for plant engineering, yet existing resources on phosphorylation are limited to model plants such as Arabidopsis, beyond which their applicability is unclear.
To expand the range of uses for these resources, the research group set out to determine the degree to which phosphorylation mechanisms are conserved across two very different plant species: Arabidopsis, from the family of flowering plants known as dicotyledons (dicots), and rice, from the family known as monocotyledons (monocots). Their large-scale analysis on rice, the first ever, identified a total of 3393 different types of proteins regulated by phosphorylation and their phosphorylation sites, of which more than half, they showed, are shared by Arabidopsis.
The surprising discovery that these two very different plants exhibit significant similarities in their mechanisms of phosphorylation suggests that information on the "phosphoproteome" of one species can be applied to others, greatly contributing to applications in plant engineering.
Data leading to the discovery has been made available to the public in an open-access database, the Plant Phosphoproteome Database, released online on May 12.
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