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Regulation of Nod1 by Hsp90 chaperone complex
Author(s) -
Hahn Ji-Sook
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.07.024
Subject(s) - nod1 , hsp90 , tetratricopeptide , chaperone (clinical) , biology , nod2 , microbiology and biotechnology , heat shock protein , innate immune system , biochemistry , genetics , immune system , gene , medicine , pathology
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.