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Issue 2, 2016
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Liposome chaperon in cell-free membrane protein synthesis: one-step preparation of KcsA-integrated liposomes and electrophysiological analysis by the planar bilayer method

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Abstract

Chaperoning functions of liposomes were investigated using cell-free membrane protein synthesis. KcsA potassium channel-reconstituted liposomes were prepared directly using cell-free protein synthesis. In the absence of liposomes, all synthesized KcsA protein aggregated. In the presence of liposomes, however, synthesized KcsA spontaneously integrated into the liposome membrane. The KscA-reconstituted liposomes were transferred to the planar bilayer across a small hole in a thin plastic sheet and the channel function of KcsA was examined. The original electrophysiological activities, such as voltage- and pH-dependence, were observed. These results suggested that in cell-free membrane protein synthesis, liposomes act as chaperones, preventing aggregation and assisting in folding and tetrameric formation, thereby allowing full channel activity.

Graphical abstract: Liposome chaperon in cell-free membrane protein synthesis: one-step preparation of KcsA-integrated liposomes and electrophysiological analysis by the planar bilayer method

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Article information


Submitted
29 Jul 2015
Accepted
26 Oct 2015
First published
09 Nov 2015

Biomater. Sci., 2016,4, 258-264
Article type
Paper
Author version available

Liposome chaperon in cell-free membrane protein synthesis: one-step preparation of KcsA-integrated liposomes and electrophysiological analysis by the planar bilayer method

M. Ando, M. Akiyama, D. Okuno, M. Hirano, T. Ide, S. Sawada, Y. Sasaki and K. Akiyoshi, Biomater. Sci., 2016, 4, 258
DOI: 10.1039/C5BM00285K

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