In bacteria, reversible dimerization and oligomerization of transmembrane proteins is often essential in signal transduction, or direct regulation of enzyme activity. In this work, ToxR systems based on ToxR from Vibrio cholerae and Photobacterium profundum were used to examine the effects of high pressure up to 50 MPa on dimerization abilities and therefore on signal transduction of wild type ToxR and of ToxR with various transmembrane segments, in different membrane environments. The results of these in vivo experiments indicated, that the dimerization ability of a membrane protein (under pressure) is rather controlled by its structure than by changes in the lipid bilayer environment.
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In bacteria, reversible dimerization and oligomerization of transmembrane proteins is often essential in signal transduction, or direct regulation of enzyme activity. In this work, ToxR systems based on ToxR from Vibrio cholerae and Photobacterium profundum were used to examine the effects of high pressure up to 50 MPa on dimerization abilities and therefore on signal transduction of wild type ToxR and of ToxR with various transmembrane segments, in different membrane environments. The results...
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