title: How TriC folds tricky proteins.
abstract: How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a question of central importance. In two recent studies in Cell by Joachimiak et al. and Freund et al., a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed.
authors.affiliation: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: a.zhuravleva@leeds.ac.uk.
authors.forename: Anastasia
authors.initials: A
authors.lastname: Zhuravleva
authors.affiliation: Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: s.e.radford@leeds.ac.uk.
authors.forename: Sheena E
authors.initials: SE
authors.lastname: Radford
mesh_terms: D056404:Chaperonin Containing TCP-1 / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones; D019098:Telomerase / Q000378:metabolism*; D016615:Telomere / Q000378:metabolism*
chemical_list: D018832:Molecular Chaperones; D019098:Telomerase; C535133:WRAP53 protein, human; D056404:Chaperonin Containing TCP-1