Putative role of a 70 kDa outer-surface protein in promoting cell-surface hydrophobicity of Serratia marcescens RZ.
Serratia marcescens RZ has been previously shown to possess pronounced cell-surface hydrophobicity, as evidenced by its affinity for hydrocarbons and polystyrene. The present report suggests the involvement of a 70 kDa protein, serraphobin, in this phenomenon. The 70 kDa protein was recovered from both the cell surface and culture supernatant of hydrophobic wild-type cells, but was either totally absent or present in minor quantities in hydrophobicity-deficient mutants. Similarly, loss of hydrophobicity of RZ cells following growth at 39 degrees C was accompanied by loss of the protein. Serraphobin was capable of binding to hexadecane droplets following a brief mixing procedure, and could be desorbed by solidifying and melting the hexadecane phase.
Bar-Ness
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Maurice and Gabriela Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Israel.
Rosenberg
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D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D012706:Serratia marcescens / Q000502:physiology*; D014867:Water
D001425:Bacterial Outer Membrane Proteins; D014867:Water