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A comparative study on the phoE genes of three enterobacterial species. Implications for structure-function relationships in a pore-forming protein of the outer membrane
- Source :
- European Journal of Biochemistry. 164:469-475
- Publication Year :
- 1987
- Publisher :
- Wiley, 1987.
-
Abstract
- The cloned phoE genes from Enterobacter cloacae and Klebsiella pneumoniae are normally expressed and regulated in Escherichia coli K-12, and their products are correctly assembled into the outer membrane. Differences between the three PhoE proteins were found with binding of two out of ten monoclonal antibodies directed against the cell-surface-exposed part and in pore characteristics, but not in phage receptor function. The DNA sequences of the E. cloacae and K. pneumoniae phoE genes were determined and used to predict the primary structures of the encoded proteins. In the upstream non-coding regions, which showed more variations among the three genes than the coding regions, conserved sequences were identified which might be involved in regulation of phoE gene expression. Comparison of the predicted PhoE primary structures revealed a high degree of homology, with 81% of the amino acid residues being identical in all three proteins. Four small variable regions were found where differences are the most pronounced, corresponding to regions which were previously predicted to be exposed at the cell surface. Implications of the sequence comparison for structure-function relationships in PhoE protein are discussed.
- Subjects :
- DNA, Bacterial
Porins
Biology
medicine.disease_cause
Biochemistry
Pore forming protein
Homology (biology)
Conserved sequence
Structure-Activity Relationship
Enterobacteriaceae
Species Specificity
Genes, Regulator
Gene expression
medicine
Coding region
Amino Acid Sequence
Cloning, Molecular
Escherichia coli
Gene
Base Sequence
Biological Evolution
Molecular biology
Gene Expression Regulation
Genes, Bacterial
Bacterial outer membrane
Bacterial Outer Membrane Proteins
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 164
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....5391291617c0d899feccde4d143f425a
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1987.tb11080.x