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J. Biol. Chem., Vol. 282, Issue 8, 5608-5616, February 23, 2007

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Nonribosomal Synthesis of Fengycin on an Enzyme Complex Formed by Fengycin Synthetases^*

Cheng-Yeu Wu¹, Chyi-Liang Chen¹, Yu-Hsiu Lee, Yu-Chieh Cheng, Ying-Chung Wu, Hung-Yu Shu, Friedrich Götz, and Shih-Tung Liu²

From the Molecular Genetics Laboratory, Department of Microbiology and Immunology, Chang-Gung University, 259 Wen-Hwa 1st Road, Kwei-Shan, Taoyuan 333, Taiwan and Biologisches Institut, AG Mikrobielle Genetik, Der Universtät Tübingen, Waldhäuser Strasse 70/8, 70276 Tübingen, Germany

Fengycin, a lipopeptidic antibiotic, is synthesized nonribosomally by five fengycin synthetases (FenC, FenD, FenE, FenA, and FenB) in Bacillus subtilis F29-3. This work demonstrates that these fengycin synthetases interlock to form a chain, which coils into a 14.5-nm structure. In this chain, fengycin synthetases are linked in the order FenC-FenD-FenE-FenA-FenB by interactions between the C-terminal region of an upstream enzyme and the N-terminal region of its downstream partner enzyme, with their amino acid activation modules arranged colinearly with the amino acids in fengycin. This work also reveals that fengycin is synthesized on this fengycin synthetase chain, explaining how fengycin is synthesized efficiently and accurately. The results from this investigation demonstrate that forming a peptide synthetase complex is crucial to nonribosomal peptide synthesis.

Received for publication, October 16, 2006 , and in revised form, December 14, 2006.

^* This research was supported by Chang-Gung Memorial Hospital Grant CMRPD33004, National Science Council of the Republic of China Grant NSC 95-3112-B-182-002, Chang-Gung Molecular Medicine Research Center Grant CMRPD140041, and a grant for study visits for foreign academics to the Federal Republic of Germany from Deutscher Akademischer Austauschdienst, Germany. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables 1–3.

¹ These authors contributed equally to this work.

² To whom correspondence and reprint requests should be addressed. Tel./Fax: 886-32118292; E-mail: cgliu{at}mail.cgu.edu.tw.

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