Ohba A, Mizushima T, Katayama T, Sekimizu K
Faculty of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
FEBS Lett. 1997 Mar 10;404(2-3):125-8. doi: 10.1016/s0014-5793(97)00108-7.
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, beta-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.
