Welcome to the UPF Digital Repository

Proteome-wide observation of the phenomenon of life on the edge of solubility

Show simple item record

dc.contributor.author Vecchi, Giulia
dc.contributor.author Sormanni, Pietro
dc.contributor.author Mannini, Benedetta
dc.contributor.author Vandelli, Andrea
dc.contributor.author Tartaglia, Gian Gaetano
dc.contributor.author Dobson, Christopher M.
dc.contributor.author Hartl, F. Ulrich
dc.contributor.author Vendruscolo, Michele
dc.date.accessioned 2020-04-28T08:45:36Z
dc.date.available 2020-04-28T08:45:36Z
dc.date.issued 2020
dc.identifier.citation Vecchi G, Sormanni P, Mannini B, Vandelli A, Tartaglia GG, Dobson CM et al. Proteome-wide observation of the phenomenon of life on the edge of solubility. Proc Natl Acad Sci U S A. 2020 Jan 14; 117(2): 1015-1020. DOI: 10.1073/pnas.1910444117
dc.identifier.issn 0027-8424
dc.identifier.uri http://hdl.handle.net/10230/44353
dc.description.abstract To function effectively proteins must avoid aberrant aggregation, and hence they are expected to be expressed at concentrations safely below their solubility limits. By analyzing proteome-wide mass spectrometry data of Caenorhabditis elegans, however, we show that the levels of about three-quarters of the nearly 4,000 proteins analyzed in adult animals are close to their intrinsic solubility limits, indeed exceeding them by about 10% on average. We next asked how aging and functional self-assembly influence these solubility limits. We found that despite the fact that the total quantity of proteins within the cellular environment remains approximately constant during aging, protein aggregation sharply increases between days 6 and 12 of adulthood, after the worms have reproduced, as individual proteins lose their stoichiometric balances and the cellular machinery that maintains solubility undergoes functional decline. These findings reveal that these proteins are highly prone to undergoing concentration-dependent phase separation, which on aging is rationalized in a decrease of their effective solubilities, in particular for proteins associated with translation, growth, reproduction, and the chaperone system.
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher National Academy of Sciences
dc.relation.ispartof Proceedings of the National Academy of Sciences of the United States of America. 2020 Jan 14;117(2):1015-20
dc.rights © 2020 Giulia Vecchi et al. Published by PNAS. This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND)
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.other Proteïnes
dc.subject.other Processos patològics
dc.title Proteome-wide observation of the phenomenon of life on the edge of solubility
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1073/pnas.1910444117
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion


This item appears in the following Collection(s)

Show simple item record

Search DSpace

Advanced Search


My Account


In collaboration with Compliant to Partaking