Abstract
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.
Original language | English |
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Pages (from-to) | 125-128 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 404 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - 1997 Mar 10 |
Externally published | Yes |
Keywords
- DnaA protein
- Escherichia coli
- Gene expression
- Two-dimensional polyacrylamide gel electrophoresis
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology