Journal
PROTEIN SCIENCE
Volume 14, Issue 12, Pages 2947-2954Publisher
WILEY
DOI: 10.1110/ps.051679005
Keywords
MscL; oligomeric structure; covalently linked oligomer; structure/function studies; membrane proteins
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To obtain a gene construct for making single substitutions per channel and to determine the quaternary structure of the mechanosensitive channel MscL from Escherichia coli, covalent oligomers (monomer to hexamer) were engineered by gene fusion; up to six copies of the mscL gene were fused in tandem. All the multimeric tandem constructs yielded functional channels with wild-type conductance and dwell times. Importantly, only the covalent pentamer opened at the same relative pressure (compared to the pressure required to open MscS) as the wild-type MscL channel. The in vivo data strongly suggest that pentameric MscL represents the functional state of the channel.
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