Disease relevance of adiA

• Molecular characterization of adiY, a regulatory gene which affects expression of the biodegradative acid-induced arginine decarboxylase gene (adiA) of Escherichia coli [1].

High impact information on adiA

• Transcription of adiA and adiC was found to be dependent on AdiY, anaerobiosis, and acidic pH [2].
• The arginine decarboxylase system (including adi and its regulators cysB and adiY) was responsible for arginine-dependent acid resistance [3].
• During the course of a separate study, we isolated a plasmid that enhanced adi expression [4].
• We obtained a number of these mutants and examined the effects of these mutations on the acid induction of adi and cad gene expression [4].
• Biodegradative arginine decarboxylase is inducible by acid and is derepressed in an hns mutant [5].

Chemical compound and disease context of adiA

• The environmentally responsive biodegradative arginine (adi) and lysine (cad) decarboxylases are maximally induced when Escherichia coli is cultured under acidic, anaerobic conditions in rich medium [6].
• Effect of the local anesthetics phenethyl alcohol and procaine on hns mutants of the acid-induced biodegradative arginine (adi) and lysine (cad) decarboxylases of Escherichia coli [6].

Biological context of adiA

• The arginine decarboxylase system is maximally induced under conditions of acidic pH, anaerobiosis and rich medium, and AdiY was found to increase the expression of adiA [1].
• The DNA sequence of a 3-kb fragment of the Escherichia coli chromosome encoding biodegradative arginine decarboxylase was determined [7].
• The effects of the local anesthetics phenethyl alcohol (PEA) and procaine (both environmental perturbants) were investigated with lacZ operon fusions to either adi or cad and their respective hns mutants [6].

Associations of adiA with chemical compounds

• Induction of adi in the presence of sublethal concentrations of novobiocin or coumermycin A1, inhibitors of DNA gyrase, was dramatically decreased, indicating that DNA supercoiling is involved in adi expression [7].

Other interactions of adiA

• Transcriptional fusions between fragments upstream of adi and lacZ, primer extension, and site-directed mutagenesis experiments defined the pH-regulated promoter [7].
• Arginine decarboxylase (encoded by adi) is induced under conditions of acidic pH, anaerobiosis, and rich medium [7].

References