Molecular Characterization of a cDNA that Encodes Glutamate-1-semialdehyde-2,1-aminomutase in Tomato

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  • 1 Dept. of Horticulture and the Interdepartmental Plant Physiology Major, Iowa State Univ., Ames, IA 50011-1100

Our recent research has focused on the control of genes and enzymes involved with the synthesis of chlorophyll, especially as it relates to tomato fruit development and ripening. Glutamate-1-semialdehyde-2,1-aminomutase (GSAAM) is one of the first committed enzymes in the chlorophyll biosynthetic pathway, and it is one of three enzymes that catalyze the conversion of glutamate into 5-aminolevulinic acid. We have isolated a full-length cDNA clone of GSAAM from a tomato fruit library. The tomato primary sequence shows extensive homology to GSAAM sequences found in other plant species. The primary structure also predicts a 46.7-kDa, 437-amino acid, mature protein and a transit peptide of 44 amino acids. Southern analysis indicated that GSAAM was present as a single copy. Northern blot analysis showed that GSAAM was expressed differentially in various tomato organs and that GSAAM transcripts decreased with increased fruit age. Immunoblot analysis also indicated that GSAAM protein decreased dramatically with increased fruit age. These results show that there is developmental regulation of the expression of GSAAM in tomato fruits.

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