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@ARTICLE{Guo:434710,
      author       = {Guo, Emily Z. and Desrosiers, Daniel C. and Zalesak, Jan
                      and Tolchard, James and Berbon, Mélanie and Habenstein,
                      Birgit and Marlovits, Thomas and Loquet, Antoine and Galán,
                      Jorge E.},
      title        = {{A} polymorphic helix of a {S}almonella needle protein
                      relays signals defining distinct steps in type {III}
                      secretion},
      journal      = {PLoS biology},
      volume       = {17},
      number       = {7},
      issn         = {1545-7885},
      address      = {Lawrence, KS},
      publisher    = {PLoS},
      reportid     = {PUBDB-2020-00264},
      pages        = {e3000351 -},
      year         = {2019},
      abstract     = {Type III protein-secretion machines are essential for the
                      interactions of many pathogenic or symbiotic bacterial
                      species with their respective eukaryotic hosts. The core
                      component of these machines is the injectisome, a
                      multiprotein complex that mediates the selection of
                      substrates, their passage through the bacterial envelope,
                      and ultimately their delivery into eukaryotic target cells.
                      The injectisome is composed of a large cytoplasmic complex
                      or sorting platform, a multiring base embedded in the
                      bacterial envelope, and a needle-like filament that
                      protrudes several nanometers from the bacterial surface and
                      is capped at its distal end by the tip complex. A
                      characteristic feature of these machines is that their
                      activity is stimulated by contact with target host cells.
                      The sensing of target cells, thought to be mediated by the
                      distal tip of the needle filament, generates an activating
                      signal that must be transduced to the secretion machine by
                      the needle filament. Here, through a multidisciplinary
                      approach, including solid-state NMR (SSNMR) and cryo
                      electron microscopy (cryo-EM) analyses, we have identified
                      critical residues of the needle filament protein of a
                      Salmonella Typhimurium type III secretion system that are
                      involved in the regulation of the activity of the secretion
                      machine. We found that mutations in the needle filament
                      protein result in various specific phenotypes associated
                      with different steps in the type III secretion process. More
                      specifically, these studies reveal an important role for a
                      polymorphic helix of the needle filament protein and the
                      residues that line the lumen of its central channel in the
                      control of type III secretion.},
      cin          = {CSSB-UKE / CSSB-UKE-TM},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-UKE-20141216 /
                      I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31260457},
      UT           = {WOS:000478922100013},
      doi          = {10.1371/journal.pbio.3000351},
      url          = {https://bib-pubdb1.desy.de/record/434710},
}