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

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.

journal_name

EMBO Rep

journal_title

EMBO reports

authors

van Dalen A,Schrempf H,Killian JA,de Kruijff B

doi

10.1093/embo-reports/kvd067

keywords:

subject

Has Abstract

pub_date

2000-10-01 00:00:00

pages

340-6

issue

4

eissn

1469-221X

issn

1469-3178

journal_volume

1

pub_type

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