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Metabolism and Enzymology

Polygalacturonase Isozymes and Pectin Depolymerization in Transgenic rin Tomato Fruit ¹

Mann Laboratory, Department of Vegetable Crops, University of California, Davis, California 95616, Department of Plant Biology, University of California, Berkeley, California 94720

We have previously described the construction and expression of a chimeric gene that allows developmentally regulated expression of tomato (Lycopersicon esculentum) polygalacturonase in ripening-impaired, mutant (rin) tomato fruit (JJ Giovannoni, D DellaPenna, AB Bennett, RL Fischer [1989] The Plant Cell 1: 53-63). We now show that expression of the chimeric polygalacturonase gene in rin tomato fruit resulted in the accumulation of all three polygalacturonase isozymes (PG1, PG2A, and PG2B). Polyuronide solubilization and polyuronide depolymerization both reached their maximal levels in transgenic rin fruit prior to the appearance of PG2 isozymes. These results demonstrate that PG1, PG2A, and PG2B all arise by differential processing of a single gene product and further suggest that the PG1 isozyme is sufficient to carry out both polyuronide solubilization and depolymerization in vivo.

¹ Supported by U.S. Department of Agriculture Competitive Research Grant Office grant 89-37261-4641.

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