The tyrosine repressor negatively regulates aroH expression in Escherichia coli.
The levels of the tryptophan-sensitive isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli, encoded by the aroH gene, were elevated in tyrR and/or trpR mutants. The effect of tyrR and trpR lesions on aroH expression was confirmed by using a lacZ reporter system. The mutational elimination of either repressor led to a threefold increase in beta-galactosidase.
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907-6799.
G K
GK
Muday
D I
DI
Johnson
R L
RL
Somerville
K M
KM
Herrmann
D010723:3-Deoxy-7-Phosphoheptulonate Synthase / Q000235:genetics*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D007527:Isoenzymes / Q000235:genetics*; D008969:Molecular Sequence Data; D012045:Regulatory Sequences, Nucleic Acid; D012097:Repressor Proteins / Q000235:genetics; D014443:Tyrosine; D001616:beta-Galactosidase / Q000032:analysis
D029968:Escherichia coli Proteins; D007527:Isoenzymes; D012097:Repressor Proteins; C069256:TyrR protein, E coli; D014443:Tyrosine; D010723:3-Deoxy-7-Phosphoheptulonate Synthase; D001616:beta-Galactosidase