ArticleChannels (Austin, Tex.)
Genetic selection of activatory mutations in KcsA.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 15 citations in OpenAlex.
- Hydrophobic and lipid-mediated gating mechanism revealed by low-conductance MthK mutants.bioRxiv : the preprint server for biology · 2026Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Review
- Review
- Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.Journal of chemical information and modeling · 2015Article
- Using yeast to study potassium channel function and interactions with small molecules.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Probing the energy landscape of activation gating of the bacterial potassium channel KcsA.PLoS computational biology · 2013Article
- Timothy mutation disrupts the link between activation and inactivation in Ca(V)1.2 protein.The Journal of biological chemistry · 2011Article
- Genetic screen for potassium leaky small mechanosensitive channels (MscS) in Escherichia coli: recognition of cytoplasmic β domain as a new gating element.The Journal of biological chemistry · 2011Article
- Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.The Journal of biological chemistry · 2010Article
- Design and characterization of a constitutively open KcsA.FEBS letters · 2010Article
- A molecular mechanism for proton-dependent gating in KcsA.FEBS letters · 2010Article
- Searching for interesting channels: pairing selection and molecular evolution methods to study ion channel structure and function.Molecular bioSystems · 2009Review
- Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.Channels (Austin, Tex.)Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The KcsA potassium channel from Streptomyces lividans is one of the most actively studied ion channels. However, there are still unresolved issues about its gating mechanism in vivo because the channel is only activated by highly acidic intracellular pH, meaning that it will be mostly inactive in its host environment. In this study we have used a genetic complementation assay of K+-auxotrophic E. coli (TK2420) and S. cerevisiae (SGY1528) to identify activatory or 'gain-of-function' mutations which allow functional activity of KcsA in the physiological environment of two markedly different expression systems. These mutations clustered at the helix-bundle-crossing in both TM1 and TM2 (residues H25, L105, A108, T112, W113, F114, E118 and Q119), and include residues previously implicated in the pH-gating mechanism. We discuss how these gain-of-function mutations may result in their activatory phenotype, the relative merits of the E. coli and S. cerevisiae genetic complementation approaches for the identification of gating mutations in prokaryotic K+ channels, and ways in which this assay may be improved for future use in screening protocols.
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