Journal
CHEMISTRY & BIOLOGY
Volume 21, Issue 8, Pages 923-934Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2014.06.004
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Funding
- Bureau of Science, Technology, and Innovation Policy, Cabinet Office, Government of Japan
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- New Energy and Industrial Technology Development Organization of Japan
- Grants-in-Aid for Scientific Research [25108706] Funding Source: KAKEN
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JBIR-34 and -35 produced by Streptomyces sp. Sp080513GE-23 are nonribosomal peptides that possess an unusual 4-methyloxazoline moiety. Through draft genome sequencing, cosmid cloning, and gene disruption, the JBIR-34 and -35 biosynthesis gene cluster (fmo cluster) was identified; it encodes 20 proteins including five nonribosomal peptide synthetases (NRPSs). Disruption of one of these NRPS genes (fmoA3) resulted in no JBIR-34 and -35 production and accumulation of 6-chloro4- hydroxyindole-3-carboxylic acid. Stable isotope-feeding experiments indicated that the methyl group of the methyloxazoline ring is derived from alanine rather than methionine. A recombinant FmoH protein, a glycine/serine hydroxymethyltransferase homolog, catalyzed conversion of alpha-methyl-L-serine into D-alanine (the reverse reaction of alpha-methyl-Lserine synthesis catalyzed by FmoH in vivo). Taken together, we concluded that alpha-methyl-L-serine synthesized from D-alanine is incorporated into JBIR34 and -35 to form the 4-methyloxazoline moiety. We also propose the biosynthesis pathway of JBIR34 and -35.
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