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THE PLANT CELL, Vol 8, Issue 11 2139-2150, Copyright © 1996 by American Society of Plant Biologists
A Polyketide Synthase Is Required for Fungal Virulence and Production of the Polyketide T-Toxin
G. Yang, M. S. Rose, B. G. Turgeon and O. C. Yoder
Department of Plant Pathology, 334 Plant Science Building, Cornell University, Ithaca, New York 14853
Race T of the fungal pathogen Cochliobolus heterostrophus is highly
virulent toward Texas male sterile (T) maize and differs from its relative,
race O, at a locus (Tox1) that is responsible for the production of
T-toxin, a family of linear long-chain (C35 to C41) polyketides. In a
previous study, the restriction enzyme-mediated integration procedure was
used to mutagenize and tag Tox1. Here, we report that the DNA recovered
from the insertion site of one mutant encodes a 7.6-kb open reading frame
(2530 amino acids) that identifies a multifunctional polyketide synthase
(PKS)-encoding gene (PKS1) with six catalytic domains arranged in the
following order, starting at the N terminus: [beta]-ketoacyl synthase,
acyltransferase, dehydratase, enoyl reductase, [beta]-ketoacyl reductase,
and acyl carrier protein. PKS1 is interrupted by four apparent introns (74,
57, 49, and 41 bp) and exists in the genome as a single copy surrounded by
highly repetitive, A+T-rich DNA. When PKS1 in race T was inactivated by
targeted gene disruption, T-toxin production and high virulence were
eliminated, indicating that this PKS is required for fungal virulence. Race
O strains, which do not produce T-toxin, lack a detectable homolog of PKS1,
suggesting that race T may have acquired PKS1 by horizontal transfer of DNA
rather than by vertical inheritance from an ancestral strain.
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