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GrainGenes Reference Report: PNA-87-4169

Reference	PNA-87-4169
Title	Primary structure of a key enzyme in plant tetrapyrrole synthesis glutamate 1-semialdehyde aminotransferase
Journal	Proceedings of the National Academy of Sciences, USA
Year	1990
Volume	87
Pages	4169-4173
Author	Grimm B
Type	Article
Language	English
Abstract	The formation of .delta.-aminolevulinate from glutamate 1- semialdehyde (GSA) is catalyzed by glutamate 1-semialdehyde aminotransferase (EC 5.4.3.8). The active form of the barley enzyme appears to be a dimer of identical subunits with a molecular mass of 46 kDa. From the purified enzyme, amino acid sequences of the N- terminal ends of the mature protein as well as an internal peptide were determined. DNA primers deduced from these peptide sequences were used to amplify with the polymerase chain reaction a cDNA sequence encoding part of the enzyme. Screening a cDNA library with this DNA fragment identified a full-length clone encoding the 49,540-Da precursor of the GSA aminotransferase. The transit peptide for chloroplast import consists of 34 amino acids. GSA aminotransferase and a precursor form were expressed on a multicopy plasmid in Escherichia coli. Both recombinant gene products reacted wtih an antibody against the barley GSA aminotransferase. Active barley GSA aminotransferase expressed in E. coli was shown to be active in assays of bacterial cell extracts. As a gene symbol for barley GSA aminotransferase, GSA is proposed.
Keyword	Barley Chlorophyll Escherichia-coli Expression

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