Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
Copyright policy )Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
The Arabidopsis protein RPM1 activates disease resistance in response to Pseudomonas syringae proteins targeted to the inside of the host cell via the bacterial type III delivery system. We demonstrate that specific mutations in the ATP-binding domain of a single Arabidopsis cytosolic HSP90 isoform compromise RPM1 function. These mutations do not affect the function of related disease resistance proteins. RPM1 associates with HSP90 in plant cells. The Arabidopsis proteins RAR1 and SGT1 are required for the action of many R proteins, and display some structural similarity to HSP90 co-chaperones. Each associates with HSP90 in plant cells. Our data suggest that (i) RPM1 is an HSP90 client protein; and (ii) RAR1 and SGT1 may function independently as HSP90 cofactors. Dynamic interactions among these proteins can regulate RPM1 stability and function, perhaps similarly to the formation and regulation of animal steroid receptor complexes.
- Universitat Politècnica de València Spain
- University of North Carolina at Chapel Hill United States
- John Innes Centre United Kingdom
- Western University Canada
- Spanish National Research Council Spain
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Arabidopsis Proteins, Molecular Sequence Data, Arabidopsis, Intracellular Signaling Peptides and Proteins, Pseudomonas syringae, Cell Cycle Proteins, Models, Biological, Mutagenesis, Animals, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Carrier Proteins, Plant Proteins
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Arabidopsis Proteins, Molecular Sequence Data, Arabidopsis, Intracellular Signaling Peptides and Proteins, Pseudomonas syringae, Cell Cycle Proteins, Models, Biological, Mutagenesis, Animals, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Carrier Proteins, Plant Proteins
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