{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ciesielski SJ"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS","National Science Center, Poland"],"pagination":["1465-1477"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11209805"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["598(12)"],"pubmed_abstract":["J-domain proteins are critical Hsp70 co-chaperones. A and B types have a poorly understood glycine-rich region (G<sub>rich</sub>) adjacent to their N-terminal J-domain (J<sub>dom</sub>). We analyzed the ability of J<sub>dom</sub>/G<sub>rich</sub> 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<sub>rich</sub> 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<sub>rich</sub>-Hsp70 interaction of Classes A and B J-domain proteins can fine tune the activity of Hsp70, thus be"],"journal":["FEBS letters"],"pubmed_title":["Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70."],"pmcid":["PMC11209805"],"funding_grant_id":["R35 GM127009","OPUS 21 2021/41/B/NZ8/02835","P41 GM136463"],"pubmed_authors":["Stolarska M","Schilke BA","Tonelli M","Ciesielski SJ","Tomiczek B","Craig EA"],"additional_accession":[]},"is_claimable":false,"name":"Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70.","description":"J-domain proteins are critical Hsp70 co-chaperones. A and B types have a poorly understood glycine-rich region (G<sub>rich</sub>) adjacent to their N-terminal J-domain (J<sub>dom</sub>). We analyzed the ability of J<sub>dom</sub>/G<sub>rich</sub> 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<sub>rich</sub> 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<sub>rich</sub>-Hsp70 interaction of Classes A and B J-domain proteins can fine tune the activity of Hsp70, thus be","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-06-03T07:33:15.075Z","creation":"2026-04-26T03:09:44.433Z"},"accession":"S-EPMC11209805","cross_references":{"pubmed":["38529663"],"doi":["10.1002/1873-3468.14857"]}}