Physicochemical determinants of chaperone requirements.
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.
Tartaglia
Gian Gaetano
GG
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Dobson
Christopher M
CM
Hartl
F Ulrich
FU
Vendruscolo
Michele
M
D018834:Chaperonin 60 / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D012995:Solubility
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones