Folding and aggregation of export-defective mutants of the maltose-binding protein.
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.
Betton
Jean-Michel
JM
Unité de Repliement et de Modélisation des Protéines, Institut Pasteur, CNRS-URA 2185, Paris, France. jmbetton@pasteur.fr
Phichith
Denis
D
Hunke
Sabine
S
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
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C461619:MalE protein, E coli; D033902:Periplasmic Binding Proteins; D021382:Protein Sorting Signals