J. Biochem, 1989, Vol. 106, No. 1 5-7
© 1989 Japanese Biochemical Society
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Phosphorylation of a Bacterial Activator Protein, OmpR, by a Protein Kinase, EnvZ, Results in Stimulation of Its DNA-Binding Ability1
*Laboratory of Microbiology, School of Agriculture, Nagoya University Chikusa-ku, Nagoya, Aichi 464
**Institute of Applied Microbiology, The University of Tokyo Bunkyo-ku, Tokyo 113
2To whom correspondence should be addressed.
The Escherichia coli OmpR protein is an activator protein specific for the ompF and ompC genes, which respectively encode the outer membrane proteins, OmpF and OmpC. The EnvZ protein is a protein kinase specific for the OmpR protein. In this study, we compared the in vitro DNA-binding ability of the phosphorylated form of the OmpR protein with that of the non-phosphorylated form by means of non-denaturing gel retardation analysis and DNase I footprinting analysis. The results indicate that the phosphorylation of the OmpR protein results in stimulation of its in vitro DNA-binding ability as to both the ompF and ompC promoter DNAs.
1This study was supported by a Grant-in-Aid for Scientific Research (6160001) from the Ministry of Education, Science and Culture of Japan.
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