Construction of hybrid plasmids containing the lysA gene of Escherichia coli: studies of expression in Escherichia coli and Saccharomyces cerevisiae.
The lysA gene of Escherichia coli has been cloned from a lambda transducing phage on various plasmids, present in different copy numbers in bacterial cells. Synthesis of the product of this gene, diaminopimelate (DAP)-decarboxylase, and its regulation have been studied. Expression does not follow a simple gene dosage effect, maximal expression already being obtained with a six-copy plasmid. This result suggests that either a positive or an autogenous regulatory mechanism is involved. We also used one of the hybrid plasmids to look for expression of the bacterial lysA gene in Saccharomyces cerevisiae. The results indicate that the product of the E. coli gene is not actively translated in yeast.
D001426:Bacterial Proteins; D010582:Bacteriophage lambda / Q000235:genetics; D002262:Carboxy-Lyases / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D005822:Genetic Vectors; D008239:Lysine / Q000235:genetics*; D009876:Operon; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D013045:Species Specificity
D001426:Bacterial Proteins; D002262:Carboxy-Lyases; C079912:LysA protein, Bacteria; C020031:diaminopimelic acid decarboxylase; D008239:Lysine