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R K Taylor

Publications and source records attributed to R K Taylor.

59 records · Page 4Linked to original sources
PubMed1983

Isolation and characterization of mutations altering expression of the major outer membrane porin proteins using the local anaesthetic procaine.

Mutations at several different chromosomal locations affect expression of the major outer membrane porin proteins (OmpF and OmpC) of Escherichia coli K12. Those that map at 21 and 47 minutes define the structural genes for OmpF and OmpC, respectively. A third locus, ompB, is defined by mutations that map at 74 minutes. The ompB locus contains two genes whose products regulate the relative amounts of ompF and ompC expression. One of these genes, ompR, encodes a positive regulatory protein that interacts at the ompF and ompC promoters. Mutations in ompR exhibit an OmpF- OmpC- or an OmpF+ OmpC- phenotype. The product of the second gene, envZ, affects regulation of the porin proteins in an unknown manner. Previously isolated mutations in envZ exhibit an OmpF- OmpC+ phenotype and also have pleiotropic effects on other exported proteins. In the presence of local anaesthetics such as procaine, wild-type strains exhibit properties similar to these envZ mutants, i.e. OmpF- OmpC+. Using ompF-lac fusion strains, we have exploited this procaine effect to isolate two new classes of envZ mutations. One of these classes exhibits an OmpF+ OmpC- phenotype. The other allows expression of both OmpF and OmpC but alters the relative amounts found under various growth conditions. Like previously isolated envZ mutations, these also affect regulation of other exported proteins, such as lambda receptor. These results permit a more detailed analysis of the omp regulon and they may shed light on one of the mechanisms by which local anaesthetics exert their effect.

Bacterial Outer Membrane Proteins↗
PubMed1983

Benign recurrent aseptic meningitis (Mollaret's meningitis). A case report.

Benign recurrent aseptic meningitis is a rare disorder described by Mollaret in 1944. Since then cases have been reported in the European and American literature, and the first report on a case in South Africa appeared recently. In this article a case seen in Durban is reported and the characteristic manifestations and differential diagnosis are briefly reviewed.

Adult↗
PubMed1983

Isolation and characterization of chain-terminating nonsense mutations in a porin regulator gene, envZ.

We isolated four independent amber mutations in gene envZ, whose product is involved in the regulation of porin protein genes ompF and ompC. The envZ amber strains exhibit an OmpF-/+ OmpC- porin phenotype and express other envelope protein genes at wild-type levels. This phenotype is clearly different from that of the previously isolated class of envZ mutants that exhibit an OmpF- OmpC+ phenotype and a pleiotropic decrease in the expression of several exported protein genes, including lamB and phoA. The addition of the local anesthetic procaine to wild-type strains also causes a pleiotropic decrease in the expression of genes ompF, lamB, and phoA. However, procaine has no effect on the synthesis of LamB or PhoA protein in the envZ amber strains. Thus, although EnvZ protein is required for the full expression of ompF and ompC, it apparently is not normally involved in the expression of other envelope protein genes. One interpretation of these results is that the EnvZ protein can be altered either by mutation or by procaine to a form that interferes with the expression of several envelope protein genes other than ompF and ompC. Finally, complementation analysis with ompR insertion mutations supports the physical data of Mizuno et al. (J. Biol. Chem 257:13692-13698, 1982) that suggest that envZ is cotranscribed with ompR from a single promoter in the order ompR envZ.

Bacterial Outer Membrane Proteins↗
PubMed1981

Identification of OmpR: a positive regulatory protein controlling expression of the major outer membrane matrix porin proteins of Escherichia coli K-12.

We report here on the cloning of a gene located within the ompB locus of E. coli K-12. This gene, designated ompR, resides on a 10.9-kilobase EcoRI fragment that we cloned, using a lambda vector and in vitro packaging techniques. By subcloning portions of this fragment into the high-copy-number plasmid pBR322, we have isolated the ompR gene on a 1.4-kilobase EcoRI-AvaI fragment. This fragment has been characterized physically and will facilitate a more detailed study of the role and mechanism of porin regulation by the ompB locus.

Bacterial Proteins↗