Single Residue Substitutions that Change the Gating Properties of a Mechanosensitive Channel in Escherichia coli
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...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 93; no. 21; pp. 11652 - 11657 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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National Academy of Sciences of the United States of America
15.10.1996
National Acad Sciences National Academy of Sciences |
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Abstract | 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 core spanning two-thirds of the molecule and a more hydrophilic carboxyl terminal tail. Because MscL had no homology to characterized proteins, it was impossible to predict functional regions of the protein by simple inspection. Here, by mutagenesis, we have searched for functionally important regions of this molecule. We show that a short deletion from the amino terminus (3 amino acids), and a larger deletion of 27 amino acids from the carboxyl terminus of this protein, had little if any effect in channel properties. We have thus narrowed the search of the core mechanosensitive mechanism to 106 residues of this 136-amino acid protein. In contrast, single residue substitutions of a lysine in the putative first transmembrane domain or a glutamine in the periplasmic loop caused pronounced shifts in the mechano-sensitivity curves and/or large changes in the kinetics of channel gating, suggesting that the conformational structure in these regions is critical for normal mechanosensitive channel gating. |
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AbstractList | 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 core spanning two-thirds of the molecule and a more hydrophilic carboxyl terminal tail. Because MscL had no homology to characterized proteins, it was impossible to predict functional regions of the protein by simple inspection. Here, by mutagenesis, we have searched for functionally important regions of this molecule. We show that a short deletion from the amino terminus (3 amino acids), and a larger deletion of 27 amino acids from the carboxyl terminus of this protein, had little if any effect in channel properties. We have thus narrowed the search of the core mechanosensitive mechanism to 106 residues of this 136-amino acid protein. In contrast, single residue substitutions of a lysine in the putative first transmembrane domain or a glutamine in the periplasmic loop caused pronounced shifts in the mechano-sensitivity curves and/or large changes in the kinetics of channel gating, suggesting that the conformational structure in these regions is critical for normal mechanosensitive channel gating. Blount et al show that a short deletion from the amino terminus and a large deletion of 27 amino acids from the carboxyl terminus of an MscL protein had little effect in channel properties. |
Audience | PUBLIC |
Author | Schroeder, Matthew J. Blount, Paul Nagle, Scott K. Sukharev, Sergei I. Kung, Ching |
AuthorAffiliation | Laboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA |
AuthorAffiliation_xml | – name: Laboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA |
Author_xml | – sequence: 1 givenname: Paul surname: Blount fullname: Blount, Paul – sequence: 2 givenname: Sergei I. surname: Sukharev fullname: Sukharev, Sergei I. – sequence: 3 givenname: Matthew J. surname: Schroeder fullname: Schroeder, Matthew J. – sequence: 4 givenname: Scott K. surname: Nagle fullname: Nagle, Scott K. – sequence: 5 givenname: Ching surname: Kung fullname: Kung, Ching |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8876191$$D View this record in MEDLINE/PubMed |
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Snippet | 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... Blount et al show that a short deletion from the amino terminus and a large deletion of 27 amino acids from the carboxyl terminus of an MscL protein had little... |
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SubjectTerms | 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 |
Title | Single Residue Substitutions that Change the Gating Properties of a Mechanosensitive Channel in Escherichia coli |
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