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Journal of Bacteriology, August 2009, p. 4916-4923, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00407-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Biosynthesis of Aliphatic Polyketides by Type III Polyketide Synthase and Methyltransferase in Bacillus subtilis{triangledown} ,{dagger}

Chiaki Nakano, Hiroki Ozawa,{ddagger} Genki Akanuma, Nobutaka Funa, and Sueharu Horinouchi*

Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan

Received 26 March 2009/ Accepted 19 May 2009

Type III polyketide synthases (PKSs) synthesize a variety of aromatic polyketides in plants, fungi, and bacteria. The bacterial genome projects predicted that probable type III PKS genes are distributed in a wide variety of gram-positive and -negative bacteria. The gram-positive model microorganism Bacillus subtilis contained the bcsA-ypbQ operon, which appeared to encode a type III PKS and a methyltransferase, respectively. Here, we report the characterization of bcsA (renamed bpsA, for Bacillus pyrone synthase, on the basis of its function) and ypbQ, which are involved in the biosynthesis of aliphatic polyketides. In vivo analysis demonstrated that BpsA was a type III PKS catalyzing the synthesis of triketide pyrones from long-chain fatty acyl-coenzyme A (CoA) thioesters as starter substrates and malonyl-CoA as an extender substrate, and YpbQ was a methyltransferase acting on the triketide pyrones to yield alkylpyrone methyl ethers. YpbQ thus was named BpsB because of its functional relatedness to BpsA. In vitro analysis with histidine-tagged BpsA revealed that it used broad starter substrates and produced not only triketide pyrones but also tetraketide pyrones and alkylresorcinols. Although the aliphatic polyketides were expected to localize in the membrane and play some role in modulating the rigidity and properties of the membrane, no detectable phenotypic changes were observed for a B. subtilis mutant containing a whole deletion of the bpsA-bpsB operon.

* Corresponding author. Mailing address: Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81-3-58415123. Fax: 81-3-58418021. E-mail: asuhori{at}mail.ecc.u-tokyo.ac.jp

{triangledown} Published ahead of print on 22 May 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

{ddagger} Present address: Pharmaceutical Research Laboratories, Ajinomoto Co., Inc., Kawasaki-ku, Kanagawa 210-8681, Japan.

Journal of Bacteriology, August 2009, p. 4916-4923, Vol. 191, No. 15
0021-9193/09/$08.00+0     doi:10.1128/JB.00407-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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