An in vivo screen reveals protein-lipid interactions crucial for gating a mechanosensitive channel.

ABSTRACT: The bacterial mechanosensitive channel MscL is the best-studied mechanosensor, thus serving as a paradigm of how a protein senses and responds to mechanical force. Models for the transition of Escherichia coli MscL from closed to open states propose a tilting of the transmembrane domains in the plane of the membrane, suggesting dynamic protein-lipid interactions. Here, we used a rapid in vivo assay to assess the function of channels that were post-translationally modified at several different sites in a region just distal to the cytoplasmic end of the second transmembrane helix. We utilized multiple probes with various affinities for the membrane environment. The in vivo functional data, combined with site-directed mutagenesis, single-channel analyses, and tryptophan fluorescence measureme

SUBMITTER: Iscla I 

PROVIDER: S-EPMC3023395 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature