title: The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.
abstract: Autotransporters are single polypeptides consisting of an outer membrane translocation domain mediating the translocation of a passenger domain. The periplasmic folding state of the passenger domain is controversial. By comparisons of passenger domains differing in their folding properties, our results suggest that periplasmic folding of passenger domains interferes with translocation.
authors.affiliation: Canada Research Chair on Bacterial Animal Diseases, Université de Montréal, Faculté de Médecine Vétérinaire, 3200 Sicotte, St.-Hyacinthe, J2S 7C6 Quebec, Canada.
authors.forename: Nancy
authors.initials: N
authors.lastname: Rutherford
authors.forename: Marie-Eve
authors.initials: ME
authors.lastname: Charbonneau
authors.forename: Frédéric
authors.initials: F
authors.lastname: Berthiaume
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Betton
authors.forename: Michael
authors.initials: M
authors.lastname: Mourez
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D018844:Cyclin-Dependent Kinases / Q000378:metabolism; D003545:Cysteine; D026901:Membrane Transport Proteins / Q000378:metabolism*; D017510:Protein Folding; D021381:Protein Transport
chemical_list: D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D018844:Cyclin-Dependent Kinases; D000469:Alkaline Phosphatase; D003545:Cysteine