EFFECTS OF MULTICOPY LEUO ON THE EXPRESSION OF THE ACID-INDUCIBLE LYSINE DECARBOXYLASE GENE IN ESCHERICHIA-COLI

We previously reported that mutations in hns, the structural gene for the histone like protein H-NS, cause derepressed expression of cadA, which encodes the acid-inducible lysine decarboxylase at noninducing pH (pH 8.0). This study reports the characterization of a plasmid isolated from an Escherichia coli library that suppresses the effect of an hns mutation on cadA expression. A previously sequenced open reading frame, leuO, proves to be the gene that causes the hns-complementing phenotype. The mechanism for this phenotype appears to be overexpression of leuO from a multicopy plasmid, which drastically reduces production of CadC, the essential activator for cadA induction, These results show an in vivo regulatory phenotype for leuO, consistent with its proposed protein sequence.