title: Chaperomics: in vivo GroEL function defined.
abstract: A recent proteome analysis of protein folding inside cells of Escherichia coli predicts that only 84 of the approximately 2400 cytosolic proteins expressed in minimal media depend absolutely on the GroEL/GroES chaperone system to avoid aggregation. These proteins are enriched in alpha/beta domains and 13 are essential for growth.
authors.affiliation: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK. jellis@bio.warwick.ac.uk
authors.forename: R John
authors.initials: RJ
authors.lastname: Ellis
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D040901:Proteomics / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D018834:Chaperonin 60; D018832:Molecular Chaperones; D046912:Multiprotein Complexes