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Journal of Bacteriology, May 2000, p. 2978-2981, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

FabG, an NADPH-Dependent 3-Ketoacyl Reductase of Pseudomonas aeruginosa, Provides Precursors for Medium-Chain-Length Poly-3-Hydroxyalkanoate Biosynthesis in Escherichia coli

Qun Ren,dagger Nicolas Sierro, Bernard Witholt,* and Birgit Kessler

Institute of Biotechnology, ETH Hönggerberg, CH-8093 Zürich, Switzerland

Received 22 October 1999/Accepted 3 February 2000

Escherichia coli hosts expressing fabG of Pseudomonas aeruginosa showed 3-ketoacyl coenzyme A (CoA) reductase activity toward R-3-hydroxyoctanoyl-CoA. Furthermore, E. coli recombinants carrying the poly-3-hydroxyalkanoate (PHA) polymerase-encoding gene phaC in addition to fabG accumulated medium-chain-length PHAs (mcl-PHAs) from alkanoates. When E. coli fadB or fadA mutants, which are deficient in steps downstream or upstream of the 3-ketoacyl-CoA formation step during beta -oxidation, respectively, were transformed with fabG, higher levels of PHA were synthesized in E. coli fadA, whereas similar levels of PHA were found in E. coli fadB, compared with those of the corresponding mutants carrying phaC alone. These results strongly suggest that FabG of P. aeruginosa is able to reduce mcl-3-ketoacyl-CoAs generated by the beta -oxidation to 3-hydroxyacyl-CoAs to provide precursors for the PHA polymerase.

* Corresponding author. Mailing address: Institute of Biotechnology, ETH Honggerberg, CH-8093 Zurich, Switzerland. Phone: 41.1.6333286. Fax: 41.1.6331051. E-mail: bw{at}biotech.biol.ethz.ch.

dagger Present address: Institute of Microbiology, ETH Zentrum, CH-8092 Zürich, Switzerland.

Journal of Bacteriology, May 2000, p. 2978-2981, Vol. 182, No. 10
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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