Please use this identifier to cite or link to this item:
https://hdl.handle.net/1959.11/15568
Title: | 'In Silico' Identification of Carboxylate Clamp Type Tetratricopeptide Repeat Proteins in 'Arabidopsis' and Rice As Putative Co-Chaperones of Hsp90/Hsp70 | Contributor(s): | Prasad, Bishun D (author); Goel, Shilpi (author); Krishna, Priti (author) | Publication Date: | 2010 | Open Access: | Yes | DOI: | 10.1371/journal.pone.0012761 | Handle Link: | https://hdl.handle.net/1959.11/15568 | Abstract: | The essential eukaryotic molecular chaperone Hsp90 operates with the help of different co-chaperones, which regulate its ATPase activity and serve as adaptors to recruit client proteins and other molecular chaperones, such as Hsp70, to the Hsp90 complex. Several Hsp90 and Hsp70 co-chaperones contain the tetratricopeptide repeat (TPR) domain, which interacts with the highly conserved EEVD motif at the C-terminal ends of Hsp90 and Hsp70. The acidic side chains in EEVD interact with a subset of basic residues in the TPR binding pocket called a 'carboxylate clamp'. Since the carboxylate clamp residues are conserved in the TPR domains of known Hsp90/Hsp70 co-chaperones, we carried out an in silico search for TPR proteins in 'Arabidopsis' and rice comprising of at least one three-motif TPR domain with conserved amino acid residues required for Hsp90/Hsp70 binding. This approach identified in Arabidopsis a total of 36 carboxylate clamp (CC)-TPR proteins, including 24 novel proteins, with potential to interact with Hsp90/Hsp70. The newly identified CC-TPR proteins in 'Arabidopsis' and rice contain additional protein domains such as ankyrin, SET, octicosapeptide/Phox/Bem1p (Phox/PB1), DnaJ-like, thioredoxin, FBD and F-box, and protein kinase and U-box, indicating varied functions for these proteins. To provide proof-of-concept of the newly identified CC-TPR proteins for interaction with Hsp90, we demonstrated interaction of AtTPR1 and AtTPR2 with AtHsp90 in yeast two-hybrid and 'in vitro' pull down assays. These findings indicate that the 'in silico' approach used here successfully identified in a genome-wide context CC-TPR proteins with potential to interact with Hsp90/Hsp70, and further suggest that the Hsp90/Hsp70 system relies on TPR co-chaperones more than it was previously realized. | Publication Type: | Journal Article | Source of Publication: | PLoS One, 5(9), p. 1-18 | Publisher: | Public Library of Science | Place of Publication: | United States of America | ISSN: | 1932-6203 | Fields of Research (FoR) 2008: | 060702 Plant Cell and Molecular Biology | Socio-Economic Objective (SEO) 2008: | 820402 Rice | Peer Reviewed: | Yes | HERDC Category Description: | C1 Refereed Article in a Scholarly Journal |
---|---|
Appears in Collections: | Journal Article |
Files in This Item:
File | Description | Size | Format |
---|
Items in Research UNE are protected by copyright, with all rights reserved, unless otherwise indicated.