We identified proteins whose amounts were altered in a temperature-sensitive dnaA46 mutant of Escherichia coli. Proteins whose amounts were increased in the mutant were serine hydroxymethyltransferase, β-ketoacyl [acyl carrier protein] synthase II, long-chain fatty acid transport protein, and UDP-glucose 4-epimerase, while the decreased ones were flagellin and D-ribose-binding protein. Transformation of the mutant with a plasmid containing the wild type dnaA gene complemented the phenotype. As pulse-labeling experiments revealed that the rates of synthesis of the proteins were altered in the mutant, DnaA protein may be involved in expression of these proteins.
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