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Construction of lac fusions to the inducible arginine‐and lysine decarboxylase genes of Escherichia coli K12
Author(s) -
Auger E. A.,
Redding K. E.,
Plumb T.,
Childs L. C.,
Meng S.Y.,
Bennett G. N.
Publication year - 1989
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1989.tb00208.x
Subject(s) - lysine decarboxylase , escherichia coli , lysine , arginine decarboxylase , biology , arginine , carboxy lyases , biochemistry , gene , enzyme , amino acid , putrescine , cadaverine
Summary The induction of several amino acid decarboxylases under anaerobic conditions at low pH has been known for many years, but the mechanism associated with this type of regulation has not been elucidated. To study the regulation of the biodegradative arginine and lysine decarboxylases of Escherichia coli K12, Mudlac fusions to these genes were isolated. Mudlac fusion strains deficient for lysine decarboxylase or arginine decarboxylase were identified using decarboxylase indicator media and analysed for their regulation of β‐galactosidase expression. The position of the Mud‐lac fusion in lysine decarboxylase‐deficient strains has been mapped to the cadA gene at 93.7 minutes, while the Mudlac fusions exhibiting a deficiency in the inducible arginine decarboxylase have been mapped to 93.4 minutes.