J-domain proteins are critical Hsp70 co-chaperones. A and B types have a poorly understood glycine-rich region (G) adjacent to their N-terminal J-domain (J). We analyzed the ability of J/G segments of yeast Class B Sis1 and a suppressor variant of Class A, Ydj1, to rescue the inviability of sis1-∆. In each, we identified a cluster of G residues required for rescue. Both contain conserved hydrophobic and acidic residues and are predicted to form helices. While, as expected, the Sis1 segment docks on its J-domain, that of Ydj1 does not. However, data suggest both interact with Hsp70. We speculate that the G-Hsp70 interaction of Classes A and B J-domain proteins can fine tune the activity of Hsp70, thus being particularly important for the function of Class B.
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| http://dx.doi.org/10.1002/1873-3468.14857 | DOI Listing |
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