Abstract
The mechanosensitive channel of large conductance (MscL) is a homooligomeric, stretch activated membrane protein responsible for regulating osmotic pressure in bacteria and archaea. Increasing membrane tension activates the protein resulting in a ∼2.9 nS non-selective pore. Two MscL crystal structures have been solved in distinct conformations and oligomeric states. M. tuberculosis MscL is a non-conducting pentamer while S. aureus MscL is a partially expanded tetramer. The primary sequences of these proteins are 38% identical and 57% similar. Given their high relatedness, the structures raise interesting questions regarding the assembly and activation of MscL homologs. We have been interested in understanding the molecular determinants responsible for the differences between the two structures, specifically the switch between tetrameric and pentameric species. Using a combination of multi-angle light scattering and mass tagging followed by Blue Native PAGE, we have characterized the oligomeric states of several MscL homologs and chimeras. We find that the two methods are in good agreement with each other and single molecule measurements. Potential reasons for the differences in oligomeric states will be discussed.
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