Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors

Zhang, Minghao, Kadota, Yasuhiro, Prodromou, Chrisostomos, Shirasu, Ken and Pearl, Laurence H (2010) Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors. Molecular Cell, 39 (2). pp. 269-281. ISSN 1097-2765

Full text not available from this repository.

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 Ran l 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.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Subjects: Q Science
Depositing User: Chrisostomos Prodromou
Date Deposited: 06 Feb 2012 20:34
Last Modified: 10 Jul 2013 10:07
URI: http://sro.sussex.ac.uk/id/eprint/26664
📧 Request an update