title: Folding and aggregation of export-defective mutants of the maltose-binding protein.
abstract: We previously characterized a defective-folding variant of the periplasmic maltose-binding protein, MalE31. To examine the alternative folding pathways open to the MalE31 precursor, we have analyzed the cellular fates of this aggregation-prone protein carrying altered signal sequences. Our results are most easily interpreted by a kinetic competition between exportation, folding, and degradation.
authors.affiliation: Unité de Repliement et de Modélisation des Protéines, Institut Pasteur, CNRS-URA 2185, Paris, France. jmbetton@pasteur.fr
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Betton
authors.forename: Denis
authors.initials: D
authors.lastname: Phichith
authors.forename: Sabine
authors.initials: S
authors.lastname: Hunke
mesh_terms: D001692:Biological Transport; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014644:Genetic Variation; D006360:Heat-Shock Proteins / Q000378:metabolism; D018869:Heat-Shock Response; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D021382:Protein Sorting Signals / Q000235:genetics; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C461619:MalE protein, E coli; D033902:Periplasmic Binding Proteins; D021382:Protein Sorting Signals