% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Viennet:862750,
      author       = {Viennet, Thibault and Bungert-Plümke, Stefanie and Elter,
                      Shantha and Viegas, Aldino and Fahlke, Christoph and
                      Etzkorn, Manuel},
      title        = {{R}econstitution and {NMR} {C}haracterization of the
                      {I}on-{C}hannel {A}ccessory {S}ubunit {B}arttin in
                      {D}etergents and {L}ipid-{B}ilayer {N}anodiscs},
      journal      = {Frontiers in molecular biosciences},
      volume       = {6},
      issn         = {2296-889X},
      address      = {Lausanne},
      publisher    = {Frontiers},
      reportid     = {FZJ-2019-02992},
      pages        = {13},
      year         = {2019},
      abstract     = {Barttin is an accessory subunit of ClC-K chloride channels
                      expressed in the kidney and the inner ear. Main functions of
                      ClC-K/barttin channels are the generation of the
                      cortico-medullary osmotic gradients in the kidney and the
                      endocochlear potential in the inner ear. Mutations in the
                      gene encoding barttin, BSND, result in impaired urinary
                      concentration and sensory deafness. Barttin is predicted to
                      be a two helical integral membrane protein that directly
                      interacts with its ion channel in the membrane bilayer where
                      it stabilizes the channel complex, promotes its
                      incorporation into the surface membrane and leads to channel
                      activation. It therefore is an attractive target to address
                      fundamental questions of intermolecular communication within
                      the membrane. However, so far inherent challenges in protein
                      expression and stabilization prevented comprehensive in
                      vitro studies and structural characterization. Here we
                      demonstrate that cell-free expression enables production of
                      sufficient quantities of an isotope-labeled barttin variant
                      (I72X Barttin, capable to promote surface membrane insertion
                      and channel activation) for NMR-based structural studies.
                      Additionally, we established purification protocols as well
                      as reconstitution strategies in detergent micelles and
                      phospholipid bilayer nanodiscs. Stability, folding, and NMR
                      data quality are reported as well as a suitable assignment
                      strategy, paving the way to its structural
                      characterization.},
      cin          = {ICS-6 / ICS-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ICS-4-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30931313},
      UT           = {WOS:000463667700001},
      doi          = {10.3389/fmolb.2019.00013},
      url          = {https://juser.fz-juelich.de/record/862750},
}