Molecular cloning of the 5-aminolevulinic acid dehydratase gene from Rhodobacter sphaeroides

Abstract

A hemB mutant of Escherichia coli was used to clone the gene encoding 5-aminolevulinic acid dehydratase from Rhodobacter sphaeroides after physiological complementation of the mutation. A 2.9-kb DNA fragment was obtained and cloned in both orientations into the unique PstI restriction site of pUC19. This recombinant plasmid encodes a protein (Mr 39,000) that is immunoreactive with antibodies raised against the enzyme from higher plants.

Toxicology and molecular biology of δ‐aminolevulinate dehydratase

“…Currently, ALA dehydratase cDNA has been cloned from ten species, i.e., human [19], rat [21], mouse [22], bovine [MI, E. coli [6,23], M. sociabilis [24], R. sphaeroides [31], yeast [lo], pea [25] and spinach [26]. When the amino acid sequences of ALA dehydratase from mammals [18,19,21,221 were compared with those of higher plants [25,261, the latter were found to have a special amino-terminal region, which has the characteristics of a membrane-spanning domain ( Fig.…”