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EMBO Rep. 2011 Jun 17;12(8):804-10. doi: 10.1038/embor.2011.102.

The role of trimerization in the osmoregulated betaine transporter BetP.

Author information

1
Department of Structural Biology, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany.

Abstract

The osmoregulated betaine transporter BetP is a stable trimer. Structural studies have shown that individual protomers can adopt distinct transport conformations, implying a functional role for the trimeric state in transport, although the role of trimerization in regulation is not yet understood. We designed putative monomeric mutants by molecular-dynamics simulations and in silico alanine-scanning mutagenesis. Several mutants including BetP-W101A/T351A were monomeric in detergent as well as in the membrane, as shown by blue native gel electrophoresis, crosslinking and electron microscopy. This monomeric form retains the ability to accumulate betaine, but is no longer regulated by hyperosmotic shock.

PMID:
21681199
PMCID:
PMC3147255
DOI:
10.1038/embor.2011.102
[Indexed for MEDLINE]
Free PMC Article

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