ArticleEMBO reports2000
Efficient membrane assembly of the KcsA potassium channel in Escherichia coli requires the protonmotive force.
Article in EMBO reports, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Synthesis and Evaluation of a Library of Alternating Amphipathic Copolymers to Solubilize and Study Membrane Proteins.Biomacromolecules · 2022Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling.Journal of biomolecular NMR · 2015Article
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- Article
- The role of extramembranous cytoplasmic termini in assembly and stability of the tetrameric K(+)-channel KcsA.The Journal of membrane biology · 2010Article
- Inactivation of the KcsA potassium channel explored with heterotetramers.The Journal of general physiology · 2010Article
- Article
- A conserved function of YidC in the biogenesis of respiratory chain complexes.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Very little is known about the biogenesis and assembly of oligomeric membrane proteins. In this study, the biogenesis of KcsA, a prokaryotic homotetrameric potassium channel, is investigated. Using in vivo pulse-chase experiments, both the monomeric and tetrameric form could be identified. The conversion of monomers into a tetramer is found to be a highly efficient process that occurs in the Escherichia coli inner membrane. KcsA does not require ATP hydrolysis by SecA for insertion or tetramerization. The presence of the proton-motive force (pmf) is not necessary for transmembrane insertion of KcsA; however, the pmf proved to be essential for the efficiency of oligomerization. From in vivo and in vitro experiments it is concluded that the electrical component, deltapsi, is the main determinant for this effect. These results demonstrate a new role of the pmf in membrane protein biogenesis.
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Registered trials
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