Nitration of a peptide phytotoxin by bacterial nitric oxide synthase

Johan A. Kers, Michael J. Wach, Stuart B. Krasnoff, Joanne Widom, Kimberly D. Cameron, Raghida A. Bukhalid, Donna M. Gibson, Brian R. Crane and Rosemary Loria ()
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Johan A. Kers: Cornell University
Michael J. Wach: Cornell University
Stuart B. Krasnoff: Cornell University
Joanne Widom: Cornell University
Kimberly D. Cameron: Cornell University
Raghida A. Bukhalid: Cornell University
Donna M. Gibson: Agricultural Research Service, United States Department of Agriculture
Brian R. Crane: Cornell University
Rosemary Loria: Cornell University

Nature, 2004, vol. 429, issue 6987, 79-82

Abstract: Abstract Nitric oxide (NO) is a potent intercellular signal in mammals that mediates key aspects of blood pressure, hormone release, nerve transmission and the immune response of higher organisms1,2,3,4. Proteins homologous to full-length mammalian nitric oxide synthases (NOSs) are found in lower multicellular organisms5. Recently, genome sequencing has shown that some bacteria contain genes coding for truncated NOS proteins; this is consistent with reports of NOS-like activities in bacterial extracts6,7. Biological functions for bacterial NOSs are unknown, but have been presumed to be analogous to their role in mammals. Here we describe a gene in the plant pathogen Streptomyces turgidiscabies that encodes a NOS homologue, and we reveal its role in nitrating a dipeptide phytotoxin required for plant pathogenicity8. High similarity between bacterial NOSs indicates a general function in biosynthetic nitration; thus, bacterial NOSs constitute a new class of enzymes9,10,11. Here we show that the primary function of Streptomyces NOS is radically different from that of mammalian NOS. Surprisingly, mammalian NO signalling and bacterial biosynthetic nitration share an evolutionary origin.

Date: 2004
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DOI: 10.1038/nature02504

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