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The role of trimerization in the osmoregulated betaine transporter BetP
Author(s) -
Perez Camilo,
Khafizov Kamil,
Forrest Lucy R,
Krämer Reinhard,
Ziegler Christine
Publication year - 2011
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2011.102
Subject(s) - betaine , trimer , mutagenesis , mutant , osmotic shock , monomer , biochemistry , in silico , transporter , alanine scanning , aquaporin , alanine , chemistry , biology , dimer , amino acid , gene , organic chemistry , polymer
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.

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