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Protein Science (2005), 14:2947-2954. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Engineering covalent oligomers of the mechanosensitive channel of large conductance from Escherichia coli with native conductance and gating characteristics

Joost H.A. Folgering, Justina C. Wolters and Bert Poolman

Department of Biochemistry, Groninger Biomolecular Sciences and Biotechnology Institute, and Materials Science Centreplus (MSCplus), University of Groningen, 9747 AG, Groningen, The Netherlands

(RECEIVED June 30, 2005; FINAL REVISION September 23, 2005; ACCEPTED September 27, 2005)

To obtain a gene construct for making single substitutions per channel and to determine the quaternary structure of the mechanosensitive channel MscL from Escherichia coli, covalent oligomers (monomer to hexamer) were engineered by gene fusion; up to six copies of the mscL gene were fused in tandem. All the multimeric tandem constructs yielded functional channels with wild-type conductance and dwell times. Importantly, only the covalent pentamer opened at the same relative pressure (compared to the pressure required to open MscS) as the wild-type MscL channel. The in vivo data strongly suggest that pentameric MscL represents the functional state of the channel.

Keywords: MscL; oligomeric structure; covalently linked oligomer; structure/function studies; membrane proteins

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051679005.

Reprint requests to: Bert Poolman, Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands; e-mail: B.Poolman{at}rug.nl; fax: +31-50-3634165.


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G. van den Bogaart, V. Krasnikov, and B. Poolman
Dual-Color Fluorescence-Burst Analysis to Probe Protein Efflux through the Mechanosensitive Channel MscL
Biophys. J., February 15, 2007; 92(4): 1233 - 1240.
[Abstract] [Full Text] [PDF]


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