Open AccessExpression from the Escherichia coli dapA promoter is regulated by intracellular levels of diaminopimelic acid
Author(s) -
Acord John,
Masters Millicent
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09577.x
Subject(s) - diaminopimelic acid , escherichia coli , lysine , biosynthesis , biology , biochemistry , enzyme , bacteria , amino acid , enterobacteriaceae , gene , microbiology and biotechnology , peptidoglycan , genetics
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 ( I 0.5 = 10 μM ), 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 (P dapA ) increases in response to diaminopimelic acid limitation in E. coli K‐12.