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Journal of Bacteriology, September 1999, p. 5426-5432, Vol. 181, No. 17
Department of Microbiology and Immunology,
University of British Columbia, Vancouver, British Columbia V6T 1Z3,
Canada,1 and Department of Biology,
Georgia State University, Atlanta, Georgia 30302-40382
Received 29 January 1999/Accepted 23 June 1999
Pseudomonas aeruginosa can utilize arginine and other
amino acids as both carbon and nitrogen sources. Earlier studies have shown that the specific porin OprD facilitates the diffusion of basic
amino acids as well as the structurally analogous beta-lactam antibiotic imipenem. The studies reported here showed that the expression of OprD was strongly induced when arginine, histidine, glutamate, or alanine served as the sole source of carbon. The addition
of succinate exerted a negative effect on induction of oprD, likely due to catabolite repression. The
arginine-mediated induction was dependent on the regulatory protein
ArgR, and binding of purified ArgR to its operator upstream of the
oprD gene was demonstrated by gel mobility shift and DNase
assays. The expression of OprD induced by glutamate as the carbon
source, however, was independent of ArgR, indicating the presence of
more than a single activation mechanism. In addition, it was observed
that the levels of OprD responded strongly to glutamate and alanine as
the sole sources of nitrogen. Thus, that the expression of
oprD is linked to both carbon and nitrogen metabolism of
Pseudomonas aeruginosa.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Amino Acid-Mediated Induction of the Basic Amino
Acid-Specific Outer Membrane Porin OprD from Pseudomonas
aeruginosa
*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada. Phone: (604) 822-2682. Fax: (604)
822-6041. E-mail: bob{at}cmdr.ubc.ca.
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