Asc locus for resistance to Alternaria stem canker in tomato does not encode the enzyme aspartate

The fungal disease resistance locus Alternaria stem canker (Asc) in tomato has been suggested to encode the enzyme aspartate carbamoyltransferase (AC Tase). To test this hypothesis a segment of the tomato ACTase gene was amplified by the polymerase chain reaction (PCR) using degenerate primers. The PCR product obtained was subsequently used to isolate an ACTase cDNA clone. Restriction fragment length polymorphism (RFLP) linkage analysis showed that the AC Tase gene and the Asc locus do not cosegregate. RFLP mapping positioned the ACTase gene on chromosome 11, while the Asc locus is located on chromosome 3. These results exclude the possibility that the ACTase protein is encoded by the Asc locus.

[1]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[2]  G. Martin,et al.  High density molecular linkage maps of the tomato and potato genomes. , 1992, Genetics.

[3]  S. Briggs,et al.  Reductase activity encoded by the HM1 disease resistance gene in maize. , 1992, Science.

[4]  M. Kater,et al.  cDNA cloning and expression of Brassica napus enoyl-acyl carrier protein reductase in Escherichia coli , 1991, Plant Molecular Biology.

[5]  R. Verkerk,et al.  Acid phosphatase-11, a tightly linked molecular marker for root-knot nematode resistance in tomato: from protein to gene, using PCR and degenerate primers containing deoxyinosine , 1991, Plant Molecular Biology.

[6]  M. Haring,et al.  The use of transgenic plants to understand transposition mechanisms and to develop transposon tagging strategies , 1991, Plant Molecular Biology.

[7]  J. Hille,et al.  Tomato resistance to Alternaria stem canker: localization in host genotypes and functional expression compared to non-host resistance , 1989, Theoretical and Applied Genetics.

[8]  D. Evans,et al.  Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[9]  J. Souciet,et al.  The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activity and nuclear localization. , 1989, The Journal of biological chemistry.

[10]  M. Jacquet,et al.  Molecular characterization of a Dictyostelium discoideum gene encoding a multifunctional enzyme of the pyrimidine pathway. , 1989, European journal of biochemistry.

[11]  D. Lipman,et al.  Improved tools for biological sequence comparison. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[12]  M. Daly,et al.  MAPMAKER: an interactive computer package for constructing primary genetic linkage maps of experimental and natural populations. , 1987, Genomics.

[13]  D. Gilchrist.  Interaction of the asc locus in f 8 paired lines of tomato with Alternaria alternata f. sp. lycopersici and AAL-toxin , 1987 .

[14]  B. Jarry,et al.  The rudimentary gene of Drosophila melanogaster encodes four enzymic functions. , 1987, Journal of molecular biology.

[15]  J. Turner.  Activities of ribulose-1,5-bisphosphate carboxylase and glutamine synthetase in isolated mesophyll cells exposed to tabtoxin , 1986 .

[16]  G. Church,et al.  Genomic sequencing. , 1993, Methods in molecular biology.

[17]  James B. Hicks,et al.  A plant DNA minipreparation: Version II , 1983, Plant Molecular Biology Reporter.

[18]  J. Turner.  Tabtoxin, produced by Pseudomonas tabaci, decreases Nicotiana tabacum glutamine synthetase in vivo and causes accumulation of ammonia. , 1981 .

[19]  A. Ferguson,et al.  Phaseolotoxin: chlorosis, ornithine accumulation and inhibition of ornithine carbamoyltransferase in different plants. , 1980 .

[20]  G. Stark,et al.  Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate. , 1971, The Journal of biological chemistry.

[21]  D. Pratt,et al.  Effects of the host-selective toxins of Alternaria alternata f.sp. lycopersici on suspension-cultured tomato cells , 1988 .

[22]  J. Daly.  The Role of Recognition in Plant Disease , 1984 .

[23]  D. Gilchrist.  Production and Nature of a Host-Specific Toxin from Alternaria alternata f. sp. lycopersici , 1976 .

[24]  R. G. Grogan.  A Stem Canker Disease of Tomato Caused by Alternaria alternata f. sp. lycopersici , 1975 .