Journal
FEBS LETTERS
Volume 579, Issue 20, Pages 4513-4519Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2005.07.024
Keywords
Chp-1; heat shock factor; Hsp90; Nod1; protein phosphatase 5
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Nod1 and Nod2 proteins play important roles in mammalian innate immune responses as intracellular sensors for bacterial peptidoglycan. Nod1 and Nod2 share structural homology with many R proteins involved in plant disease resistance. It has been demonstrated that plant Hsp90 and its co-chaperone RAR1 are implicated in R-mediated disease resistance. Here the Chp-1 gene encoding a mammalian homologue of plant RAR1 was identified as a new target for transcriptional activation by heat shock factor 1 (HSF1), a stress-responsive HSF isoform. In addition, Nod1 is demonstrated to be a client protein of the Hsp90 chaperone complex containing the Chp-1. Chp-1 interacts with the tetratricopeptide repeat (TPR) domain of protein phosphatase 5 (PP5) and the ATPase domain of Hsp90 via two distinct zinc-binding cysteine and histidine rich domains (CHORDS). These findings suggest a common regulatory mechanism involving the Hsp90 chaperone complex in R-mediated disease resistance in plants and Nod1-mediated innate immune response in mammals. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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