Single Residue Substitutions that Change the Gating Properties of a Mechanosensitive Channel in Escherichia coli

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 93; no. 21; pp. 11652 - 11657
• Main Authors: Blount, Paul, Sukharev, Sergei I., Schroeder, Matthew J., Nagle, Scott K., Kung, Ching
• Format: Journal Article
• Language: English
• Published: Legacy CDMS National Academy of Sciences of the United States of America 15.10.1996; National Acad Sciences; National Academy of Sciences
• Subjects: Amino Acid Sequence; Amino acids; Antibodies; Bacteria; Bacterial Proteins - physiology; Base Sequence; Cell Membrane - physiology; Cellular biology; Escherichia coli; Escherichia coli - genetics; Escherichia coli - physiology; Escherichia coli Proteins; Ion Channel Gating; Ion Channels - biosynthesis; Ion Channels - chemistry; Ion Channels - physiology; Kinetics; Life Sciences (General); Macromolecular Substances; Membrane Potentials; Molecular Sequence Data; Molecules; Mutagenesis; Mutagenesis, Insertional; Plasmids; Point Mutation; Protein Structure, Secondary; Proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Spheroplasts; Non-Nasa Center; Nasa Discipline Cell Biology; NASA Discipline Cell Biology; Non-NASA Center

MscL is a channel that opens a large pore in the Escherichia coli cytoplasmic membrane in response to mechanical stress. Previously, we highly enriched the MscL protein by using patch clamp as a functional assay and cloned the corresponding gene. The predicted protein contains a largely hydrophobic...