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 Repjournal_title
EMBO reportsauthors
van Dalen A,Schrempf H,Killian JA,de Kruijff Bdoi
10.1093/embo-reports/kvd067keywords:
subject
Has Abstractpub_date
2000-10-01 00:00:00pages
340-6issue
4eissn
1469-221Xissn
1469-3178journal_volume
1pub_type
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