title: Physicochemical determinants of chaperone requirements.
abstract: We describe a series of stringent relationships between abundance, solubility and chaperone usage of proteins. Based on these relationships, we show that the need of Escherichia coli proteins for the chaperonin GroEL can be predicted with 86% accuracy. Furthermore, from the observation that the abundance and solubility of proteins depend on the physicochemical properties of their amino acid sequences, we demonstrate that the requirement for GroEL can also be predicted directly from the sequences with 90% accuracy. These results indicate that the physicochemical properties of the amino acid sequences represent an essential component of the cellular quality control system that ensures the maintenance of protein homeostasis in living systems.
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors.forename: Gian Gaetano
authors.initials: GG
authors.lastname: Tartaglia
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
authors.forename: F Ulrich
authors.initials: FU
authors.lastname: Hartl
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
mesh_terms: D018834:Chaperonin 60 / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D012995:Solubility
chemical_list: D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones