A dominant mutation in Escherichia coli OmpR lies within a domain which is highly conserved in a large family of bacterial regulatory proteins

Kazuhiro Ikenaka, Kangla Tsung, Dorothy E. Comeau, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

We have fortuitously created an in-frame insertion mutation in the cloned ompR gene of Escherichia coli in the course of an experiment involving linker insertion mutagenesis. According to the DNA sequence, the mutant protein has an insertion at the 53rd amino acid residue, which replaced the original valine, with the sequence Ala-Leu-Glu. The expression level of the mutant protein, OmpRX6, in a minicell system, is similar to that of the wild-type protein and the size of the mutant is slightly larger than the wild type by approxiately 300 daltons. This mutant was completely unable to activate porin expression as the wildtype does, and in addition, this phenotype was shown to be dominant over the wild type. Comparison of the amino acid sequence of OmpRX6 with those of a family of homologous bacterial regulatory proteins revealed that the mutation lies in a domain which is highly conserved among these proteins.

Original languageEnglish (US)
Pages (from-to)538-540
Number of pages3
JournalMgg Molecular & General Genetics
Volume211
Issue number3
DOIs
StatePublished - Mar 1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics

Keywords

  • Osmoregulation
  • ompR mutation

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