Efficient membrane assembly of the KcsA potassium channel in Escherichia coli requires the protonmotive force

Autor(en): van Dalen, A
Schrempf, H 
Killian, JA
de Kruijff, B
Stichwörter: Biochemistry & Molecular Biology; Cell Biology; CHARGED RESIDUES; COAT PROTEIN; INNER MEMBRANE; K+-CHANNEL; PREPROTEIN TRANSLOCASE; PROTEIN TRANSLOCATION; SECA; SIGNAL-RECOGNITION PARTICLE; STOICHIOMETRY; STREPTOMYCES-LIVIDANS
Erscheinungsdatum: 2000
Herausgeber: WILEY-BLACKWELL
Journal: EMBO REPORTS
Volumen: 1
Ausgabe: 4
Startseite: 340
Seitenende: 346
Zusammenfassung: 
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 protonmotive 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 ii is concluded that the electrical component, Delta psi, is the main determinant for this effect. These results demonstrate a new role of the pmf in membrane protein biogenesis.
ISSN: 1469221X
DOI: 10.1093/embo-reports/kvd067

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