| http://purl.uniprot.org/citations/20856808 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20856808 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20856808 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0012761"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0012761"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Prasad B.D."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Prasad B.D."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Krishna P."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Krishna P."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Goel S."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/author | "Goel S."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/pages | "E12761"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/pages | "E12761"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/title | "In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/title | "In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70."xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/20856808 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20856808 |
| http://purl.uniprot.org/citations/20856808 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20856808 |
| http://purl.uniprot.org/citations/20856808 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20856808 |
| http://purl.uniprot.org/citations/20856808 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20856808 |