The chaperone network connected to human ribosome-associated complex.
18.01.2011
Jaiswal H, Conz C, Otto H, Wölfle T, Fitzke E, Mayer MP, Rospert S.
Mol Cell Biol. 2011;31(6):1160-73
Mammalian ribosome-associated complex (mRAC), consists of the J-domain protein MPP11 and the atypical Hsp70 homolog Hsp70L1. The properties of mRAC, and specifically its Hsp70L1 subunit, have not been analyzed until now. We have utilized a combination of methods, including knockdown of MPP11 in cell culture, phenotypic complementation of yeast deletion strains by mammalian homologs, and functional in vitro analysis, to dissect the mechanism of mRAC action. The results identify mRAC as a specific partner of Hsp70, which does not bind to the ribosome directly but is recruited by mRAC. Significant differences between RAC and mRAC with respect to their 70-homolog partners indicate general differences in the organizations of the yeast and mammalian chaperone networks.
