Malinverni, DuccioMarsili, SimoneBarducci, AlessandroDe Los Rios, Paolo2015-09-282015-09-282015-09-28201510.1371/journal.pcbi.1004262https://infoscience.epfl.ch/handle/20.500.14299/119304WOS:000357340100013Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteostasis in the cell. Hsp70s assist a myriad of cellular processes by binding unfolded or misfolded substrates during a complex biochemical cycle involving large-scale structural rearrangements. Here we show that an analysis of coevolution at the residue level fully captures the characteristic large-scale conformational transitions of this protein family, and predicts an evolutionary conserved-and thus functional-homo-dimeric arrangement. Furthermore, we highlight that the features encoding the Hsp70 dimer are more conserved in bacterial than in eukaryotic sequences, suggesting that the known Hsp70/Hsp110 hetero-dimer is a eukaryotic specialization built on a preexisting template.text::journal::journal article::research article