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Article Dans Une Revue eLife Année : 2017

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes

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Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. This versatility in function is achieved through a diverse family of J-protein cochaperones that select substrates for Hsp70. Substrate selection is further tuned by transient complexation between different classes of J-proteins, which expands the range of protein aggregates targeted by metazoan Hsp70 for disaggregation. We assessed the prevalence and evolutionary conservation of J-protein complexation and cooperation in disaggregation. We find the emergence of a eukaryote-specific signature for interclass complexation of canonical J-proteins. Consistently, complexes exist in yeast and human cells, but not in bacteria, and correlate with cooperative action in disaggregation in vitro. Signature alterations exclude some J-proteins from networking, which ensures correct J-protein pairing, functional network integrity and J-protein specialization. This fundamental change in J-protein biology during the prokaryote-to-eukaryote transition allows for increased fine-tuning and broadening of Hsp70 function in eukaryotes.
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hal-03334977 , version 1 (07-06-2022)

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Nadinath Nillegoda, Antonia Stank, Duccio Malinverni, Niels Alberts, Anna Szlachcic, et al.. Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes. eLife, 2017, 6, pp.e24560. ⟨10.7554/eLife.24560⟩. ⟨hal-03334977⟩
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