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Journal of Bacteriology, April 2004, p. 2499-2503, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2499-2503.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of Cfa1, a Monofunctional Acyl Carrier Protein Involved in the Biosynthesis of the Phytotoxin Coronatine

Heather Seidle,1 Vidhya Rangaswamy,2,{dagger} Robin Couch,1 Carol L. Bender,2 and Ronald J. Parry1*

Department of Chemistry, Rice University, Houston, Texas 77005,1 Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, Oklahoma 740782

Received 27 October 2003/ Accepted 4 January 2004

Cfa1 was overproduced in Escherichia coli and Pseudomonas syringae, and the degree of 4'-phosphopantetheinylation was determined. The malonyl-coenzyme A:acyl carrier protein transacylase (FabD) of P. syringae was overproduced and shown to catalyze malonylation of Cfa1, suggesting that FabD plays a role in coronatine biosynthesis. Highly purified Cfa1 did not exhibit self-malonylation activity.

* Corresponding author. Mailing address: Department of Chemistry, MS60, Rice University, Houston, TX 77005. Phone: (713) 348-2446. Fax: (713) 348-5155. E-mail: parry{at}rice.edu.

{dagger} Present address: Reliance Life Sciences, Jannagar 361140, Gujarat, India.

Journal of Bacteriology, April 2004, p. 2499-2503, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2499-2503.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.





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