Effect of hydrostatic pressure on the synthesis of outer membrane proteins in Escherichia coli.
We examined the effects of hydrostatic pressure on the synthesis of Escherichia coli outer membrane proteins, particularly for the osmoregulated ImpC and OmpF porins. It was found that the expression of ompC and ompF was markedly reduced during the growth at high pressure, most likely at the transcriptional level. However, the signal transduction processes through the regulatory proteins, EnvZ and OmpR, was not influenced by the environmental pressure. It was also found that the expression of a presumed novel outer membrane protein, named OmpX, was affected by both the medium osmolarity and pressure in a manner independent of the function of EnvZ and OmpR.
Nakashima
K
K
Deep Star Group, Japan Marine Science and Technology Center, Yokosuka.
Horikoshi
K
K
Mizuno
T
T
D001425:Bacterial Outer Membrane Proteins / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics; D006874:Hydrostatic Pressure; D009994:Osmolar Concentration; D018272:Porins / Q000096:biosynthesis; D014158:Transcription, Genetic / Q000235:genetics; D014508:Urea / Q000737:chemistry; D014882:Water-Electrolyte Balance
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D014508:Urea