Abstract
Summary A full-length clone that encodes tomato fruit tissue ( Lycopersicon esculentum Mill. ‘Rutgers’) glutamate-1-semialdehyde aminotransferase (GSAT; EC 5.4.3.8) was isolated and characterized. Amino acid sequence analysis showed that the tomato GSAT clone exhibited a high level of homology to the amino acid sequences of corresponding GSAT proteins from other plant species. The primary structure of GSAT consists of a 481-amino acid precursor that includes a 46.7 kilounit (kU), 437-amino acid mature protein and a transit peptide of 44 amino acids. Southern analysis showed that a single copy of the GSAT gene was present in the tomato genome. Northern analysis showed that the abundance of GSAT transcripts declined throughout tomato fruit development and ripening. GSAT protein content decreased dramatically by 25 days postanthesis, and GSAT protein was undetectable by day 45, the approximate beginning of chlorophyll loss and carotenoid synthesis. These results show that GSAT is regulated developmentally at the level of transcript accumulation. In addition, posttranscriptional regulation may occur through decreased translation or increased degradation of GSAT protein.
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