ArticleThe Journal of biological chemistry2011
Genetic screen for potassium leaky small mechanosensitive channels (MscS) in Escherichia coli: recognition of cytoplasmic β domain as a new gating element.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Mechanosensitive channel MscS is critical for termination of the bacterial hypoosmotic permeability response.The Journal of general physiology · 2023Article
- Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Interaction of the Mechanosensitive Channel, MscS, with the Membrane Bilayer through Lipid Intercalation into Grooves and Pockets.Journal of molecular biology · 2019Article
- Identification and Characterization of the Neisseria gonorrhoeae MscS-Like Mechanosensitive Channel.Infection and immunity · 2018Article
- Transmembrane TM3b of Mechanosensitive Channel MscS Interacts With Cytoplasmic Domain Cyto-Helix.Frontiers in physiology · 2018Article
- The mechanosensitive channel of small conductance (MscS) functions as a Jack-in-the box.Biochimica et biophysica acta · 2015Article
- The evolutionary 'tinkering' of MscS-like channels: generation of structural and functional diversity.Pflugers Archiv : European journal of physiology · 2015Review
- Mutations in a Conserved Domain of E. coli MscS to the Most Conserved Superfamily Residue Leads to Kinetic Changes.PloS one · 2015Article
- Article
- Arabidopsis MSL10 has a regulated cell death signaling activity that is separable from its mechanosensitive ion channel activity.The Plant cell · 2014Article
- The cytoplasmic cage domain of the mechanosensitive channel MscS is a sensor of macromolecular crowding.The Journal of general physiology · 2014Article
- Selectivity mechanisms in MscS-like channels: From structure to function.Channels (Austin, Tex.) · 2014Article
- MscS-like mechanosensitive channels in plants and microbes.Biochemistry · 2013Review
- Patch-clamp characterization of the MscS-like mechanosensitive channel from Silicibacter pomeroyi.Biophysical journal · 2013Article
- MscS inactivation: an exception rather than the rule. An extremophilic MscS reveals diversity within the family.Biophysical journal · 2013Article
- Ss-bCNGa: a unique member of the bacterial cyclic nucleotide gated (bCNG) channel family that gates in response to mechanical tension.European biophysics journal : EBJ · 2012Article
- Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Functional analysis of conserved motifs in the mechanosensitive channel homolog MscS-Like2 from Arabidopsis thaliana.PloS one · 2012Article
- Expression and characterization of the bacterial mechanosensitive channel MscS in Xenopus laevis oocytes.The Journal of general physiology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Mechanosensitive membrane channels in bacteria respond to the mechanical stretching of the membrane. They will open when bacteria are subjected to rapid osmotic down shock. MscS is a bacterial mechanosensitive channel of small conductance. It is a heptameric membrane protein whose transmembrane part, including the gate and its kinetics, has been well characterized. MscS has a large cytoplasmic domain of a cage-like shape that changes its conformation upon gating, but its involvement in gating is not understood. We screened MscS for mutations that cause potassium leak in Escherichia coli strains deficient in potassium transport systems. We did a phenotypic analysis of single and multiple mutants and recorded the single channel activities of some of them. After these analyses, we attributed the effects of a number of mutations to particular functional states of the channel. Our screen revealed that MscS leaks potassium in a desensitized and in an inactivated state. It also appeared that the lower part of TM3 (transmembrane, pore-forming helix) and the cytoplasmic β domain are tightly packed in the inactivated state but are dissociated in the open state. We attribute the TM3-β interaction to stabilization of the inactivated state in MscS and to the control of tight closure of its membrane pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.