The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation.
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.
Rutherford
Nancy
N
Canada Research Chair on Bacterial Animal Diseases, Université de Montréal, Faculté de Médecine Vétérinaire, 3200 Sicotte, St.-Hyacinthe, J2S 7C6 Quebec, Canada.
Charbonneau
Marie-Eve
ME
Berthiaume
Frédéric
F
Betton
Jean-Michel
JM
Mourez
Michael
M
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
D001426:Bacterial Proteins; D026901:Membrane Transport Proteins; D018844:Cyclin-Dependent Kinases; D000469:Alkaline Phosphatase; D003545:Cysteine