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Journal of Bacteriology, July 2001, p. 4040-4051, Vol. 183, No. 13
Plant Disease Resistance Research Unit,
Agricultural Research Service, U.S. Department of
Agriculture,2 and Department of Plant
Pathology,1 University of Wisconsin, Madison,
Wisconsin 53706
Received 20 December 2000/Accepted 10 April 2001
Ustilago maydis, the causal agent of corn smut disease,
acquires and transports ferric ion by producing the extracellular, cyclic peptide, hydroxamate siderophores ferrichrome and ferrichrome A. Ferrichrome biosynthesis likely proceeds by hydroxylation and acetylation of L-ornithine, and later steps likely involve
covalently bound thioester intermediates on a multimodular,
nonribosomal peptide synthetase. sid1 encodes
L-ornithine N5-oxygenase, which
catalyzes hydroxylation of L-ornithine, the first committed
step of ferrichrome and ferrichrome A biosynthesis in U. maydis. In this report we characterize sid2, another
biosynthetic gene in the pathway, by gene complementation, gene
replacement, DNA sequence, and Northern hybridization analysis.
Nucleotide sequencing has revealed that sid2 is located 3.7 kb upstream of sid1 and encodes an intronless polypeptide
of 3,947 amino acids with three iterated modules of an approximate
length of 1,000 amino acids each. Multiple motifs characteristic of the
nonribosomal peptide synthetase protein family were identified in each
module. A corresponding iron-regulated sid2 transcript of
11 kb was detected by Northern hybridization analysis. By contrast,
constitutive accumulation of this large transcript was observed in a
mutant carrying a disruption of urbs1, a zinc finger, GATA
family transcription factor previously shown to regulate siderophore
biosynthesis in Ustilago. Multiple GATA motifs are present
in the intergenic region between sid1 and sid2,
suggesting bidirectional transcription regulation by urbs1
of this pathway. Indeed, mutation of two of these motifs, known to be
important to regulation of sid1, altered the differential
regulation of sid2 by iron.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.13.4040-4051.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Characterization of the Ustilago maydis
sid2 Gene, Encoding a Multidomain Peptide Synthetase in the
Ferrichrome Biosynthetic Gene Cluster
*
Corresponding author. Mailing address: Department of
Plant Pathology, University of Wisconsin, 1630 Linden Dr.,
Madison, WI 53706. Phone: (608) 262-5309. Fax: (608) 262-1541. E-mail: sal{at}plantpath.wisc.edu.
Present address: Social Science Experimental Laboratory (SSEL),
Division of Social Science, Pasadena, CA 91125.
Present address: Department of Second Language Education, Faculty
of Education, McGill University, Montreal, QC, Canada H3A1Y2.
§
Present address: USDA-ARS Malt and Barley Laboratory, Madison, WI 53706.
Journal of Bacteriology, July 2001, p. 4040-4051, Vol. 183, No. 13
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.13.4040-4051.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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