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Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
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Reinhard Krämer
Published/Copyright:
May 9, 2009
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
Received: 2009-1-12
Accepted: 2009-3-28
Published Online: 2009-05-09
Published in Print: 2009-08-01
©2009 by Walter de Gruyter Berlin New York
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Keywords for this article
anionic lipids;
glycine betaine;
lipid-protein interaction;
molecular switch;
osmotic stress regulation;
structure;
transport;
trimer
Articles in the same Issue
- Guest Editorial
- Highlight: The gatekeepers of life yield their secrets
- Highlight: Membrane Transport and Communication
- First structural insights into the TpsB/Omp85 superfamily
- Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
- Structural and functional aspects of the multidrug efflux pump AcrB
- From the Sec complex to the membrane insertase YidC
- Emerging roles of mitochondrial membrane dynamics in health and disease
- Mitochondrial tRNA import – the challenge to understand has just begun
- Multiple pathways for mitochondrial protein traffic
- Challenges to our current view on chloroplasts
- Molecular interactions within the plant TOC complex
- Protein transport across the peroxisomal membrane
- On the fate of early endosomes
- ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
- Protein targeting by the signal recognition particle
- The peptide-loading complex – antigen translocation and MHC class I loading
- Protein-lipid interactions: paparazzi hunting for snap-shots
- The nanodisc: a novel tool for membrane protein studies
- NMR and EPR studies of membrane transporters
