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• W2080349370 endingPage "594" @default.
• W2080349370 startingPage "579" @default.
• W2080349370 abstract "In Escherichia coli. OmpR and EnvZ comprise a two component regulatory system that controls the relative expression of the outer membrane porin proteins. OmpF and OmpC. In this system, OmpR fnctions as a transcriptional regulator, serving as an activator of ompC, and as both an activator and a repressor of ompF. Previous evidence suggests that OmpR-mediated transcriptional activation involves direct interaction between OmpR and the C-terminal domain of the α subunit of RNA polymerase. However, it has remained unclear what region(s) of OmpR is directly involved in this proposed interaction. Moreover, little else is known about how OmpR activates transcription. To identify residues important for transcriptional activation, we screened for mutations in ompR that render the protein specifically defective in its ability to activate transcription. The isolated ompR alleles were characterized through haploid and diploid analyses at both the ompF and ompC promoters, and through an in vivo DNA binding assay. Through this approach, we have identified five amino acid residues in OmpR that are specifically required for transcriptional activation; R42, P179, E193, A196 and E197. We propose that these mutations define a region(s) in OmpR that may contact the C-terminal domain of α to mediate transcriptional activation." @default.
• W2080349370 created "2016-06-24" @default.
• W2080349370 creator A5027063685 @default.
• W2080349370 creator A5029900874 @default.
• W2080349370 date "1994-11-01" @default.
• W2080349370 modified "2023-10-18" @default.
• W2080349370 title "OmpR mutants specifically defective for transcriptional activation" @default.
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• W2080349370 doi "https://doi.org/10.1016/0022-2836(94)90033-7" @default.
• W2080349370 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7966283" @default.
• W2080349370 hasPublicationYear "1994" @default.
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