This Article Full Text Full Text (PDF) Supplemental material Other Versions of this Article: JB.00457-07v1 189/17/6487    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Clardy, J. Articles by Brady, S. F. Search for Related Content PubMed PubMed Citation Articles by Clardy, J. Articles by Brady, S. F.

Cyclic AMP Directly Activates NasP, an N-Acyl Amino Acid Antibiotic Biosynthetic Enzyme Cloned from an Uncultured ß-Proteobacterium ^,

Laboratory of Genetically Encoded Small Molecules, The Rockefeller University, 1230 York Avenue, New York, New York 10021,¹ Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, Massachusetts 02115²

Received 27 March 2007/ Accepted 13 June 2007

The cyclic AMP (cAMP)-dependent biosynthesis of N-acylphenylalanine antibiotics by NasP, an environmental DNA-derived N-acyl amino acid synthase, is controlled by an NasP-associated cyclic nucleotide-binding domain and is independent of the global cAMP signal transducer, cAMP receptor protein. A 16S rRNA gene sequence found on the same environmental DNA cosmid as NasP is most closely related to 16S sequences from ß-proteobacteria.

Published ahead of print on 22 June 2007.

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