{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Domanski P"],"funding":["National Science Center, Poland"],"pagination":["e2522403123"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12799103"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["123(2)"],"pubmed_abstract":["J-domain protein (JDP) chaperones function widely in proteostasis. Notably, eukaryotic class B JDPs of the cytosol/nucleus prevent assembly or drive disassembly of amyloid aggregates known to cause neurodegenerative diseases, yet their evolutionary origin is not known. Members of the most ubiquitous class B subgroup, canonical B (B<sup>C</sup>) JDPs, lack the signature zinc finger domain (ZnF) of the more prevalent class A JDPs, while having other key features in common. Our phylogenetic analysis revealed that B<sup>C</sup> JDPs evolved more than once from class A duplicates, losing their ZnF. The cytonuclear B<sup>C</sup>s emerged at the base of eukaryotes. Cytonuclear class B' (i.e., B'<sup>(ST)</sup>) JDPs that have a substrate binding domain of unknown origin, distinct from that of As "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Origin of class B J-domain proteins involved in amyloid transactions."],"pmcid":["PMC12799103"],"funding_grant_id":["OPUS 27; 2024/53/B/NZ1/00632","OPUS 21 2021/41/B/NZ8/02835"],"pubmed_authors":["Bury K","Stolarska M","Schilke BA","Czub J","Purzycki D","Domanski P","Wyszkowski H","Szymanska A","Klosowska AA","Tomiczek B","Kalinowska K","Marszalek J","Craig EA","Pitek M"],"additional_accession":[]},"is_claimable":false,"name":"Origin of class B J-domain proteins involved in amyloid transactions.","description":"J-domain protein (JDP) chaperones function widely in proteostasis. Notably, eukaryotic class B JDPs of the cytosol/nucleus prevent assembly or drive disassembly of amyloid aggregates known to cause neurodegenerative diseases, yet their evolutionary origin is not known. Members of the most ubiquitous class B subgroup, canonical B (B<sup>C</sup>) JDPs, lack the signature zinc finger domain (ZnF) of the more prevalent class A JDPs, while having other key features in common. Our phylogenetic analysis revealed that B<sup>C</sup> JDPs evolved more than once from class A duplicates, losing their ZnF. The cytonuclear B<sup>C</sup>s emerged at the base of eukaryotes. Cytonuclear class B' (i.e., B'<sup>(ST)</sup>) JDPs that have a substrate binding domain of unknown origin, distinct from that of As ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-15T13:32:43.697Z","creation":"2026-07-05T03:08:42.336Z"},"accession":"S-EPMC12799103","cross_references":{"pubmed":["41512017"],"doi":["10.1073/pnas.2522403123"]}}