Abstract
High hydrostatic pressure (HHP) is suggested to influence the structure and function of membranes and/or integrated proteins. We demonstrate for the first time HHP-induced dimer dissociation of membrane proteins in vivo with Vibrio cholerae ToxR variants in Escherichia coli reporter strains carrying ctx::lacZ fusions. Dimerization ceased at 20 to 50 MPa depending on the nature of the transmembrane segments rather than on changes in the ToxR lipid bilayer environment.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Artificial Gene Fusion
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Bacterial Proteins / metabolism*
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DNA-Binding Proteins / metabolism*
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Escherichia coli / genetics*
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Escherichia coli / metabolism*
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Genes, Reporter
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Hydrostatic Pressure*
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Protein Multimerization*
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Recombinant Proteins / metabolism
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Transcription Factors / metabolism*
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beta-Galactosidase / genetics
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beta-Galactosidase / metabolism
Substances
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Bacterial Proteins
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DNA-Binding Proteins
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Recombinant Proteins
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Transcription Factors
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toxR protein, bacteria
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beta-Galactosidase