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Functional overexpression and in vitro re‐association of OpuA, an osmotically regulated ABC‐transport complex from Bacillus subtilis
Author(s) -
Horn Carsten,
Bremer Erhard,
Schmitt Lutz
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.063
Subject(s) - bacillus subtilis , betaine , subfamily , biochemistry , glycine , atpase , proline , chemistry , in vitro , substrate (aquarium) , biology , amino acid , microbiology and biotechnology , biophysics , bacteria , enzyme , gene , genetics , ecology
The osmotically regulated OpuA uptake system from Bacillus subtilis is a member of the SBP‐dependent subfamily of ABC‐transporters. The functional complex, OpuA(A 2 B 2 C), catalyzes the osmotically controlled import of the compatible solutes glycine betaine and proline betaine. Here, we describe the purification of the isolated TMS, OpuAB. Stimulated ATPase activity of OpuAA by OpuAB demonstrated that OpuAB adopts a functional fold. An interaction between all subunits could be verified in detergent solution with the highest ATPase stimulation determined for the dimeric NBS in the re‐associated complex in the presence of all transport components plus substrate.