A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli

• Published in: Molecular microbiology Vol. 6; no. 6; p. 799
• Main Authors: Nagasawa, S, Tokishita, S, Aiba, H, Mizuno, T
• Format: Journal Article
• Language: English
• Published: England 01.03.1992
• Subjects: Adaptation, Biological - genetics; Amino Acid Sequence; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Base Sequence; Cloning, Molecular; DNA, Bacterial; Escherichia coli - genetics; Escherichia coli - physiology; Escherichia coli Proteins; Genes, Bacterial; Membrane Proteins - genetics; Membrane Proteins - metabolism; Molecular Sequence Data; Mutation; Phenotype; Phosphorylation; Phosphotransferases; Plasmids; Sequence Alignment; Signal Transduction - physiology
• ISSN: 0950-382X
• DOI: 10.1111/j.1365-2958.1992.tb01530.x

Expression of the Escherichia coli outer membrane porins, OmpC and OmpF, is regulated in response to changes in the medium osmolarity through the functions of the regulatory factors, EnvZ and OmpR. A 3.0 kilobase pair DNA fragment cloned from E. coli is able phenotypically to suppress the defect in ompC and ompF expression caused by an envZ deletion mutation, provided that a certain gene located in this fragment is expressed on a high copy-number plasmid. Nucleotide sequencing revealed that the putative gene encodes a protein of 102,452 Da. The deduced amino acid sequence of the protein shows a high degree of homology to those of both EnvZ and OmpR, i.e. it contains both a 'sensory kinase domain' and a 'response regulator domain' in its primary amino acid sequence. The protein identified in this study is probably a novel member of the homologous family of proteins involved in bacterial adaptive responses. Hence, the gene encoding this novel sensor-regulator protein was designated as barA (bacterial adaptive responses) and mapped at 60 min on the E. coli genetic map. The BarA protein in isolated membranes was demonstrated in vitro to undergo phosphorylation in the presence of ATP.