Ontology highlight
ABSTRACT:
SUBMITTER: Gao XC
PROVIDER: S-EPMC3285371 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Gao Xue-Chao XC Zhou Chen-Jie CJ Zhou Zi-Ren ZR Wu Meng M Cao Chun-Yang CY Hu Hong-Yu HY
The Journal of biological chemistry 20120103 8
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 inter ...[more]