EnvZ, a transmembrane environmental sensor of Escherichia coli K-12, is phosphorylated in vitro.
By fusing the transcriptional and translational start signals of lacZ to envZ, we have obtained high-level synthesis of a truncated EnvZ protein (EnvZ115) in which the first 38 amino acids of EnvZ are replaced with the first 8 amino acids of LacZ. Using this construct, we have partially purified the EnvZ115 protein and demonstrated that this protein can be phosphorylated in vitro. We suggest that phosphorylation may be an important feature of EnvZ function.
Igo
M M
MM
Department of Molecular Biology, Princeton University, New Jersey 08544.
Silhavy
T J
TJ
D000255:Adenosine Triphosphate / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005816:Genetic Complementation Test; D009097:Multienzyme Complexes; D009154:Mutation; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D009097:Multienzyme Complexes; D000255:Adenosine Triphosphate; C057843:envZ protein, E coli