{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["25(14)"],"submitter":["Samaddar M"],"pubmed_abstract":["Mitochondrial Hsp70 (mtHsp70) is essential for a vast repertoire of functions, including protein import, and requires effective interdomain communication for efficient partner-protein interactions. However, the in vivo functional significance of allosteric regulation in eukaryotes is poorly defined. Using integrated biochemical and yeast genetic approaches, we provide compelling evidence that a conserved substrate-binding domain (SBD) loop, L4,5, plays a critical role in allosteric communication governing mtHsp70 chaperone functions across species. In yeast, a temperature-sensitive L4,5 mutation (E467A) disrupts bidirectional domain communication, leading to compromised protein import and mitochondrial function. Loop L4,5 functions synergistically with the linker in modulating the alloster"],"journal":["Molecular biology of the cell"],"pagination":["2129-42"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4091826"],"repository":["biostudies-literature"],"pubmed_title":["Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation."],"pmcid":["PMC4091826"],"pubmed_authors":["D'Silva P","Goswami AV","Purushotham J","Samaddar M","Hegde P"],"additional_accession":[]},"is_claimable":false,"name":"Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation.","description":"Mitochondrial Hsp70 (mtHsp70) is essential for a vast repertoire of functions, including protein import, and requires effective interdomain communication for efficient partner-protein interactions. However, the in vivo functional significance of allosteric regulation in eukaryotes is poorly defined. Using integrated biochemical and yeast genetic approaches, we provide compelling evidence that a conserved substrate-binding domain (SBD) loop, L4,5, plays a critical role in allosteric communication governing mtHsp70 chaperone functions across species. In yeast, a temperature-sensitive L4,5 mutation (E467A) disrupts bidirectional domain communication, leading to compromised protein import and mitochondrial function. Loop L4,5 functions synergistically with the linker in modulating the alloster","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jul","modification":"2025-04-26T09:09:00.915Z","creation":"2019-03-27T01:31:51Z"},"accession":"S-EPMC4091826","cross_references":{"pubmed":["24829379"],"doi":["10.1091/mbc.E14-03-0821"]}}