| http://purl.uniprot.org/citations/22219199 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22219199 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22219199 | http://www.w3.org/2000/01/rdf-schema#comment | "The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding β-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical α-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.294728"xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.294728"xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Cao C.Y."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Cao C.Y."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Wu M."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Wu M."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Zhou C.J."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Zhou C.J."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Hu H.Y."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Hu H.Y."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Gao X.C."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Gao X.C."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Zhou Z.R."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/author | "Zhou Z.R."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/pages | "6044-6052"xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/pages | "6044-6052"xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/title | "The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation."xsd:string |
| http://purl.uniprot.org/citations/22219199 | http://purl.uniprot.org/core/title | "The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation."xsd:string |