PMID:15158272

Citation	Acord, J and Masters, M (2004) Expression from the Escherichia coli dapA promoter is regulated by intracellular levels of diaminopimelic acid. FEMS Microbiol. Lett. 235:131-7
Abstract	Dihydropicolinate synthase (DHDPS; E.C. 4.2.1.52) catalyses the first committed step of lysine biosynthesis in plants and bacteria. Plant DHDPS enzymes, which are responsible solely for lysine biosynthesis, are strongly inhibited by lysine (I0.5 =10 microM), whereas the bacterial enzymes which are less responsive or insensitive to lysine inhibition have the additional function of meso-diaminopimelate biosynthesis which is required for cell wall formation. Previous studies have suggested that expression of the Escherichia coli dapA gene, encoding DHDPS, is unregulated. We show here that this is not the case and that expression of LacZ from the dapA promoter (PdapA) increases in response to diaminopimelic acid limitation in E. coli K-12.
Links	PubMed Online version:10.1016/j.femsle.2004.04.022
Keywords	Bacterial Proteins/genetics; Cell Division; Chaperonins; Diaminopimelic Acid/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Deletion; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heat-Shock Proteins/genetics; Hydro-Lyases/genetics; Hydro-Lyases/metabolism; Promoter Regions, Genetic; Transcriptional Activation
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