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Applied and Environmental Microbiology, October 2003, p. 5935-5940, Vol. 69, No. 10
0099-2240/03/$08.00+0 DOI: 10.1128/AEM.69.10.5935-5940.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Melinda C. Wiles,2 Timothy D. Phillips,2 and Marian N. Beremand1*
Department of Plant Pathology and Microbiology,1 Department of Veterinary Anatomy and Public Health, Texas A&M University, College Station, Texas 778432
Received 5 March 2003/ Accepted 15 July 2003
We previously characterized Tri1, a gene required for hydroxylation of the C-8 position during trichothecene mycotoxin biosynthesis in Fusarium sporotrichioides NRRL 3299. Sequence analysis of the region surrounding Tri1 revealed a gene, named Tri16, which could encode an acyltransferase. Unlike the wild-type parent strain NRRL 3299, which accumulates primarily T-2 toxin along with low levels of diacetoxyscirpenol (DAS) and neosolaniol (NEO) and trace amounts of 8-propionyl-neosolaniol (P-NEO) and 8-isobutyryl-neosolaniol (B-NEO), mutants containing a disruption of Tri16 were blocked in the production of the three C-8 esterified compounds T-2 toxin, P-NEO, and B-NEO and accumulated the C-8-hydroxylated compound NEO along with secondary levels of DAS. These data indicate that Tri16 encodes an acyltransferase that catalyzes the formation of ester side groups at C-8 during trichothecene biosynthesis. We also report the presence of a Tri16 ortholog in Gibberella pulicaris R-6380 that is likely linked to a presumably inactive ortholog for Tri1.
Present address: Frost & Sullivan, San Antonio, TX 78229.
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