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

Nadinath B. Nillegoda, Antonia Stank, Duccio Malinverni, Niels Alberts, Anna Szlachcic, Alessandro Barducci, Paolo De Los Rios, Rebecca C Wade, Bernd Bukau

OnderzoeksoutputAcademicpeer review

54 Citaten (Scopus)
51 Downloads (Pure)

Samenvatting

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.

Originele taal-2English
Artikelnummere24560
Aantal pagina's28
TijdschrifteLife
Volume2017
Nummer van het tijdschrift6
DOI's
StatusPublished - 15-mei-2017
Extern gepubliceerdJa

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