Abstract

A class of proteins that were discovered to bind the immunosuppressant drug FK506, called FK506-binding proteins (FKBPs), are members of a sub-family of immunophilins. Although they were first identified in human, FKBPs exist in all three domains of life. In this report, a rice FKBP12 homolog was first identified as a biotic stress-related gene through suppression subtractive hybridization screening. By ectopically expressing OsFKBP12 in the heterologous model plant system, Arabidopsis thaliana, for functional characterization, OsFKBP12 was found to increase susceptibility of the plant to the pathogen, Pseudomonas syringae pv. tomato DC3000 (Pst DC3000). This negative regulatory role of FKBP12 in biotic stress responses was also demonstrated in the AtFKBP12-knockout mutant, which exhibited higher resistance towards Pst DC3000. Furthermore, this higher-plant FKBP12 homolog was also shown to be a negative regulator of salt tolerance. Using yeast two-hybrid tests, an ancient unconventional G-protein, OsYchF1, was identified as an interacting partner of OsFKBP12. OsYchF1 was previously reported as a negative regulator of both biotic and abiotic stresses. Therefore, OsFKBP12 probably also plays negative regulatory roles at the convergence of biotic and abiotic stress response pathways in higher plants.

Highlights

  • FK506-binding proteins (FKBPs) belong to a sub-family of immunophilins

  • We focused on characterizing the functions of this gene as it relates to defense response and stress tolerance

  • All of them are annotated as FKBP (FK506-binding protein)-type peptidyl-prolyl cis-trans isomerases (PPIases)

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Summary

Introduction

Immunophilins (including FKBPs and cyclophilins) were first described as the receptors of immunosuppressant drugs used in clinical settings to prevent graft rejection in transplantation [1]. FKBPs have been identified in all three domains of life and contain a conserved functional domain annotated with peptidyl-prolyl cis-trans isomerase (PPIase) activities (EC 5.2.1.8). This domain was thought to catalyze the cis/trans isomerization of proline residues in a polypeptide. Such activities were largely demonstrated in vitro and were thought to be associated with protein folding and maturation [3,4]

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