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Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors

DOI: 10.1016/j.molcel.2010.05.010 DOI Help
PMID: 20670895 PMID Help

Authors: Minghao Zhang (Institute of Cancer Research) , Yasuhiro Kadota (RIKEN Plant Science Center) , Chrisostomos Prodromou (Institute of Cancer Research) , Ken Shirasu (RIKEN Plant Science Center) , Laurence H. Pearl (The Institute of Cancer Research; University of Sussex)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Cell , VOL 39(2) , PAGES 269-281

State: Published (Approved)
Published: July 2010
Diamond Proposal Number(s): 6389

Open Access Open Access

Abstract: Hsp90-mediated function of NLR receptors in plant and animal innate immunity depends on the cochaperone Sgt1 and, at least in plants, on a cysteine- and histidine-rich domains (CHORD)-containing protein Rar1. Functionally, CHORD domains are associated with CS domains, either within the same protein, as in the mammalian melusin and Chp1, or in separate but interacting proteins, as in the plant Rar1 and Sgt1. Both CHORD and CS domains are independently capable of interacting with the molecular chaperone Hsp90 and can coexist in complexes with Hsp90. We have now determined the structure of an Hsp90-CS-CHORD ternary complex, providing a framework for understanding the dynamic nature of Hsp90-Rar1-Sgt1 complexes. Mutational and biochemical analyses define the architecture of the ternary complex that recruits nucleotide-binding leucine-rich repeat receptors (NLRs) by manipulating the structural elements to control the ATPase-dependent conformational cycle of the chaperone.

Journal Keywords: Arabidopsis; Arabidopsis; Caenorhabditis; Carrier; Cytoskeletal; Glucosyltransferases; HSP90; Multiprotein; Muscle; Protein; Quaternary; Protein; Tertiary; Tobacco

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Added On: 23/09/2010 09:48

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