
Putative Role of a 70 kDa Outer-surface Protein in Promoting Cell-surface Hydrophobicity of Serratia marcescens RZ
Author(s) -
Ronit Bar-Ness,
Mel Rosenberg
Publication year - 1989
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.352
H-Index - 35
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/00221287-135-8-2277
Subject(s) - serratia marcescens , hexadecane , chemistry , mutant , biophysics , cell , bacteria , polystyrene , chromatography , biochemistry , escherichia coli , biology , organic chemistry , gene , genetics , polymer
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.