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Mutations in a Conserved Domain of E. coli MscS to the Most Conserved Superfamily Residue Leads to Kinetic Changes
- Source :
- PLoS ONE, Vol 10, Iss 9, p e0136756 (2015), PLoS ONE
- Publication Year :
- 2015
- Publisher :
- Public Library of Science (PLoS), 2015.
-
Abstract
- In Escherichia coli (E. coli) the mechanosensitive channel of small conductance, MscS, gates in response to membrane tension created from acute external hypoosmotic shock, thus rescuing the bacterium from cell lysis. E. coli MscS is the most well studied member of the MscS superfamily of channels, whose members are found throughout the bacterial and plant kingdoms. Homology to the pore lining helix and upper vestibule domain of E. coli MscS is required for inclusion into the superfamily. Although highly conserved, in the second half of the pore lining helix (TM3B), E. coli MscS has five residues significantly different from other members of the superfamily. In superfamilies such as this, it remains unclear why variations within such a homologous region occur: is it tolerance of alternate residues, or does it define functional variance within the superfamily? Point mutations (S114I/T, L118F, A120S, L123F, F127E/K/T) and patch clamp electrophysiology were used to study the effect of changing these residues in E. coli MscS on sensitivity and gating. The data indicate that variation at these locations do not consistently lead to wildtype channel phenotypes, nor do they define large changes in mechanosensation, but often appear to effect changes in the E. coli MscS channel gating kinetics.
- Subjects :
- Models, Molecular
Patch-Clamp Techniques
Molecular Sequence Data
Protein domain
lcsh:Medicine
Spheroplasts
Gating
Biology
medicine.disease_cause
Mechanotransduction, Cellular
Ion Channels
Protein Structure, Secondary
Conserved sequence
Osmotic Pressure
Escherichia coli
medicine
Amino Acid Sequence
lcsh:Science
Conserved Sequence
Ion channel
Mutation
Ion Transport
Multidisciplinary
Sequence Homology, Amino Acid
Mechanosensation
Escherichia coli Proteins
lcsh:R
Gene Expression Regulation, Bacterial
Protein Structure, Tertiary
Cell biology
Kinetics
Biochemistry
Mechanosensitive channels
lcsh:Q
Ion Channel Gating
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 10
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....514d740268345cb3698f013d4e6c0b7e