Publication: Two polyketide synthase-encoding genes are required for biosynthesis of the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus
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Issued Date
2006-02-01
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ISSN
08940282
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2-s2.0-31644438873
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Mahidol University
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SCOPUS
Bibliographic Citation
Molecular Plant-Microbe Interactions. Vol.19, No.2 (2006), 139-149
Suggested Citation
Scott E. Baker, Scott Kroken, Patrik Inderbitzin, Thipa Asvarak, Bi Yu Li, Liang Shi, O. C. Yoder, B. Gillian Turgeon Two polyketide synthase-encoding genes are required for biosynthesis of the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus. Molecular Plant-Microbe Interactions. Vol.19, No.2 (2006), 139-149. doi:10.1094/MPMI-19-0139 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/22917
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Title
Two polyketide synthase-encoding genes are required for biosynthesis of the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus
Abstract
Cochliobolus heterostrophus race T, causal agent of southern corn leaf blight, requires T-toxin (a family of C35to C49polyketides) for high virulence on T-cytoplasm maize. Production of T-toxin is controlled by two unlinked loci, Tox1A and Tox1B, carried on 1.2 Mb of DNA not found in race O, a mildly virulent form of the fungus that does not produce T-toxin, or in any other Cochliobolus spp. or closely related fungus. PKS1, a polyketide synthase (PKS)-encoding gene at Tox1A, and DEC1, a decarboxylase-encoding gene at Tox1B, are necessary for T-toxin production. Although there is evidence that additional genes are required for T-toxin production, efforts to clone them have been frustrated because the genes are located in highly repeated, A+T-rich DNA. To overcome this difficulty, ligation specificity-based expression analysis display (LEAD), a comparative amplified fragment length polymorphism/gel fractionation/capillary sequencing procedure, was applied to cDNAs from a near-isogenic pair of race T (Tox1+) and race O (Tox1-) strains. This led to discovery of PKS2, a second PKS-encoding gene that maps at Tox1A and is required for both T-toxin biosynthesis and high virulence to maize. Thus, the carbon chain of each T-toxin family member likely is assembled by action of two PKSs, which produce two polyketides, one of which may act as the starter unit for biosynthesis of the mature T-toxin molecule. © 2006 The American Phytopathological Society.