title: Chaperoning ribosome assembly.
abstract: Reconstitution of bacterial ribosomes in vitro from RNA and protein constituents requires a heating step to rearrange conformation of an intermediate. In this issue of Molecular Cell, Maki et al. demonstrate that the DnaK chaperone system circumvents the requirement for heating.
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, 616 Mellon Institute, 4400 Fifth Avenue, Pittsburgh, PA 15213, USA.
authors.forename: John
authors.initials: J
authors.lastname: Woolford
mesh_terms: D029968:Escherichia coli Proteins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D012329:RNA, Bacterial / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D012329:RNA, Bacterial; D012269:Ribosomal Proteins; C063842:dnaK protein, E coli