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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacterium glutamicum

Reinhard Krämer
  • Institute of Biochemistry, University of Cologne, D-50674 Cologne, Germany
/ Christine Ziegler
  • Department of Structural Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany
Published Online: 2009-05-09 | DOI: https://doi.org/10.1515/BC.2009.068

Abstract

Activation of the osmoregulated trimeric betaine transporter BetP from Corynebacterium glutamicum was shown to depend mainly on the correct folding and integrity of its 55 amino acid long, partly α-helical C-terminal domain. Reorientation of the three C-terminal domains in the BetP trimer indicates different lipid-protein and protein-protein interactions of the C-terminal domain during osmoregulation. A regulation mechanism is suggested where this domain switches the transporter from the inactive to the active state. Interpretation of recently obtained electron and X-ray crystallography data of BetP led to a structure-function based model of C-terminal molecular switching involved in osmoregulation.

Keywords: anionic lipids; glycine betaine; lipid-protein interaction; molecular switch; osmotic stress regulation; structure; transport; trimer

Corresponding author


Received: 2009-01-12

Accepted: 2009-03-28

Published Online: 2009-05-09

Published in Print: 2009-08-01


Citation Information: Biological Chemistry. Volume 390, Issue 8, Pages 685–691, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.068, May 2009

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