A mutation in the putative CRP binding site of the dctA promoter of Salmonella enterica serovar Typhimurium enables growth with low orotate concentrations

Author:

Amin Mohammad R.12ORCID,Korchinski Lisa3,Yoneda Joshua K.12,Thakkar Rishi12ORCID,Sanson Carla L.A.3,Fitzgerald Stephen F.1ORCID,Kelln Rod A.3,Cameron Andrew D.S.12ORCID

Affiliation:

1. Department of Biology, Faculty of Science, University of Regina, Regina, SK, Canada

2. Institute for Microbial Systems and Society, Faculty of Science, University of Regina, Regina, SK, Canada

3. Department of Chemistry and Biochemistry, Faculty of Science, University of Regina, Regina, SK, Canada

Abstract

Salmonella enterica and Escherichia coli use the inner membrane transporter DctA to import the pyrimidine biosynthetic pathway intermediate orotate from the environment. To study the regulation of dctA expression, we used an S. enterica serovar Typhimurium pyrimidine auxotroph to select a mutant that could grow in an otherwise nonpermissive culture medium containing glucose and a low concentration of orotate. Whole genome sequencing revealed a point mutation upstream of dctA in the putative cyclic AMP receptor protein (CRP) binding site. The C→T transition converted the least favourable base to the most favourable base for CRP–DNA affinity. A dctA::lux transcriptional fusion confirmed that the mutant dctA promoter gained responsiveness to CRP even in the presence of glucose. Moreover, dctA expression was higher in the mutant than the wild type in the presence of alternative carbon sources that activate CRP.

Publisher

Canadian Science Publishing

Subject

Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology

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