ArticleProceedings of the National Academy of Sciences of the United States of America1996
Single residue substitutions that change the gating properties of a mechanosensitive channel in Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed.
- Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli.Nature communications · 2026Article
- The gram-positive HtrA, the protease that is also a chaperone.Journal of bacteriology · 2026Review
- Mechanosensitive channel engineering: A study on the mixing and matching of YnaI and MscS sensor paddles and pores.Nature communications · 2025Article
- Tight hydrophobic core and flexible helices yield MscL with a high tension gating threshold and a membrane area mechanical strain buffer.Frontiers in chemistry · 2023Article
- Building programmable multicompartment artificial cells incorporating remotely activated protein channels using microfluidics and acoustic levitation.Nature communications · 2022Article
- Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanical Activation of MscL Revealed by a Locally Distributed Tension Molecular Dynamics Approach.Biophysical journal · 2021Article
- Charged pore-lining residues are required for normal channel kinetics in the eukaryotic mechanosensitive ion channel MSL1.Channels (Austin, Tex.) · 2020Article
- The MscS-like channel YnaI has a gating mechanism based on flexible pore helices.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Membrane protein mediated bilayer communication in networks of droplet interface bilayers.Communications chemistry · 2020Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- An agonist of the MscL channel affects multiple bacterial species and increases membrane permeability and potency of common antibiotics.Molecular microbiology · 2019Article
- Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- An influenza-derived membrane tension-modulating peptide regulates cell movement and morphology via actin remodeling.Communications biology · 2019Article
- Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance.Scientific reports · 2018Article
- Nonpolar residues in the presumptive pore-lining helix of mechanosensitive channel MSL10 influence channel behavior and establish a nonconducting function.Plant direct · 2018Article
- Engineering a pH-Sensitive Liposomal MRI Agent by Modification of a Bacterial Channel.Small (Weinheim an der Bergstrasse, Germany) · 2018Article
- Transmembrane TM3b of Mechanosensitive Channel MscS Interacts With Cytoplasmic Domain Cyto-Helix.Frontiers in physiology · 2018Article
- Tension-activated channels in the mechanism of osmotic fitness inThe Journal of general physiology · 2017Article
- From membrane tension to channel gating: A principal energy transfer mechanism for mechanosensitive channels.Protein science : a publication of the Protein Society · 2016Review
51 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
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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