Cloning and nucleotide sequence of the Pseudomonas aeruginosa glucose‐selective OprB porin gene and distribution of OprB within the family Pseudomonadaceae
- 3 March 1994
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 220 (2) , 505-512
- https://doi.org/10.1111/j.1432-1033.1994.tb18649.x
Abstract
OprB is a glucose-selective porin known to be produced by Pseudomonas aeruginosa and Pseudomonas putida. We have cloned and sequenced the oprB gene of P. aeruginosa and obtained expression of OprB in Escherichia coli. The mature protein consists of 423 amino acid residues with a deduced molecular mass of 47597 Da. Several clusters of amino acid residues, potentially involved in the structure or function of the protein, were identified. An area of regional homology with E. coli LamB was also identified. Carbohydrate-inducible proteins, potentially homologous to OprB, were identified in several rRNA homology-group-I pseudomonads by sodium dodecyl sulfate/polyacrylamide gel electrophoresis analysis, Western immunoblotting and N-terminal amino acid sequencing. These species also contained DNA that hybridized to a P. aeruginosa oprB gene probe.Keywords
This publication has 36 references indexed in Scilit:
- Biophysical characterization of OprB, a glucose-inducible porin ofPseudomonas aeruginosaJournal of Bioenergetics and Biomembranes, 1993
- Structure of porin refined at 1.8 Å resolutionJournal of Molecular Biology, 1992
- A sugar‐specific porin, ScrY, is involved in sucrose uptake in enteric bacteriaMolecular Microbiology, 1991
- Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane proteinJournal of Molecular Biology, 1991
- Cysteine-22 and cysteine-38 are not essential for the functions of maltoporin (LamB protein)FEMS Microbiology Letters, 1989
- Mutations that alter the pore function of the ompF porin of Escherichia coli K12Journal of Molecular Biology, 1988
- Maltose transport and starch binding in phage-resistant point mutants of maltoporinJournal of Molecular Biology, 1988
- Specificity of the glucose channel formed by protein D1 of Pseudomonas aeruginosaBiochimica et Biophysica Acta (BBA) - Biomembranes, 1988
- Protein D1 — A glucose-inducible, pore-forming protein from the outer membrane ofPseudomonas aeruginosaFEMS Microbiology Letters, 1980
- Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K12 into four bandsFEBS Letters, 1975