Activation of Serratia marcescens hemolysin through a conformational change.
For Serratia marcescens, secreted hemolysin/cytotoxin is not only secreted but also activated by an outer membrane protein. Excluding posttranslational processing by mass spectrometry, the conformation of active and inactive ShlA derivatives strongly differed in electrophoretic mobilities, gel permeation chromatography, sensitivity to trypsin, circular dichroism, and intrinsic fluorescence. We concluded that ShlB interacts with ShlA during secretion and imposes a conformational change in ShlA to form the active hemolysin.
Walker
Georg
G
Mikrobiologie/Membranphysiologie, Universität Tübingen, Tübingen, Germany.
Hertle
Ralf
R
Braun
Volkmar
V
D001426:Bacterial Proteins / Q000378:metabolism*; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005453:Fluorescence; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011487:Protein Conformation; D012706:Serratia marcescens / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D008565:Membrane Proteins; C089911:ShlA protein, Serratia marcescens; C107896:ShlB protein, Serratia marcescens; D014357:Trypsin