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Journal of Bacteriology, May 1999, p. 3069-3075, Vol. 181, No. 10
Biotechnology Center for Agriculture and the
Environment, Cook College, Rutgers University, New Brunswick, New
Jersey 08901-8520
Received 28 January 1999/Accepted 10 March 1999
Two distinct regions of DNA encode the enzymes needed for phthalate
degradation by Burkholderia cepacia DBO1. A gene coding for
an enzyme (quinolinate phosphoribosyl transferase) involved in the
biosynthesis of NAD+ was identified between these two
regions by sequence analysis and functional assays. Southern
hybridization experiments indicate that DBO1 and other
phthalate-degrading B. cepacia strains have two dissimilar
genes for this enzyme, while non-phthalate-degrading B. cepacia strains have only a single gene. The sequenced gene was
labeled ophE, due to the fact that it is specifically
induced by phthalate as shown by lacZ gene fusions.
Insertional knockout mutants lacking ophE grow noticeably
slower on phthalate while exhibiting normal rates of growth on other
substrates. The fact that elevated levels of quinolinate phosphoribosyl
transferase enhance growth on phthalate stems from the structural
similarities between phthalate and quinolinate: phthalate is a
competitive inhibitor of this enzyme and the phthalate catabolic
pathway cometabolizes quinolinate. The recruitment of this gene for
growth on phthalate thus gives B. cepacia an advantage over
other phthalate-degrading bacteria in the environment.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Role of Quinolinate Phosphoribosyl Transferase in
Degradation of Phthalate by Burkholderia cepacia
DBO1
*
Corresponding author. Mailing address: Biotechnology
Center for Agriculture and the Environment, Foran Hall, 59 Dudley Rd., Cook College, Rutgers University, New Brunswick, NJ 08901-8520. Phone:
(732) 932-8165, ext. 320. Fax: (732) 932-0312. E-mail: zylstra{at}aesop.rutgers.edu.
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