Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate.
The Tar chemoreceptor of Escherichia coli is a membrane-bound sensory protein that facilitates bacterial chemotaxis in response to aspartate. The EnvZ molecule has a membrane topology similar to Tar and is a putative osmosensor that is required for osmoregulation of the genes for the major outer membrane porin proteins, OmpF and OmpC. The cytoplasmic signaling domain of Tar was replaced with the carboxyl portion of EnvZ, and the resulting chimeric receptor activated transcription of the ompC gene in response to aspartate. The activation of ompC by the chimeric receptor was absolutely dependent on OmpR, a transcriptional activator for ompF and ompC.
Utsumi
R
R
Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854.
Brissette
R E
RE
Rampersaud
A
A
Forst
S A
SA
Oosawa
K
K
Inouye
M
M
D001224:Aspartic Acid / Q000494:pharmacology*; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins; D002628:Chemoreceptor Cells; D002678:Chimera; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D005822:Genetic Vectors; D007473:Ion Channels; D009994:Osmolar Concentration; D010957:Plasmids; D018272:Porins; D015398:Signal Transduction / Q000187:drug effects*; D014158:Transcription, Genetic; D013721:Triethylenephosphoramide; D014882:Water-Electrolyte Balance
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D007473:Ion Channels; D018272:Porins; D001224:Aspartic Acid; D013721:Triethylenephosphoramide