Work

Membrane topology of the outer membrane protein OprH from Pseudomonas aeruginosa: PCR-mediated site-directed insertion and deletion mutagenesis

Year: 1996

Type: article

Abstract: The 21-kDa outer membrane protein OprH from Pseudomonas aeruginosa is overexpressed under Mg2+ starvation conditions and when overproduced causes resistance to polymyxin B, gentamicin, and EDTA. By circular dichroism analysis, OprH revealed a calculated beta-sheet structure content of 47.3%. PCR-based site-directed deletion and epitope insertion mutagenesis was used to test a topological model of OprH as an eight-stranded beta-barrel. Three permissive and seven nonpermissive malarial epitope insertion mutants and four permissive and four nonpermissive deletion mutants confirmed the general accuracy of this model. Thus, OprH is the smallest outer membrane protein to date to be confirmed as a beta-stranded protein.

Source: Journal of Bacteriology

DOI: 10.1128/jb.178.11.3346-3349.1996

Authors: B H Rehm, R E Hancock

Institution: University of British Columbia

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funder: Deutsche Forschungsgemeinschaft