title: Tethering creates unusual kinetics for ribosome-associated chaperones with nascent chains.
abstract: This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 A from the emerging nascent chain has an effective concentration of 1 x 10(-1) M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 10(4) s(-1) in order to keep chains unfolded.
authors.affiliation: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130-3932, USA. switt1@ lsuhsc.edu
authors.forename: Stephan N
authors.initials: SN
authors.lastname: Witt
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D017510:Protein Folding; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides; C476430:SSB protein, E coli; C057842:SecB protein, Bacteria; C063842:dnaK protein, E coli