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@ARTICLE{Bunduc:603156,
      author       = {Bunduc, Catalin and Ding, Y. and Kuijl, C. and Marlovits,
                      Thomas and Bitter, W. and Houben, E. N. G.},
      title        = {{R}econstitution of a minimal {ESX}-5 type {VII} secretion
                      system suggests a role for {PPE} proteins in the outer
                      membrane transport of proteins},
      journal      = {mSphere},
      volume       = {8},
      number       = {5},
      issn         = {2379-5042},
      address      = {Washington, DC},
      publisher    = {American Society for Microbiology},
      reportid     = {PUBDB-2024-00793},
      pages        = {e00402-23},
      year         = {2023},
      abstract     = {Mycobacteria utilize type VII secretion systems (T7SSs) to
                      secrete proteins across their highly hydrophobic and diderm
                      cell envelope. Pathogenic mycobacteria have up to five
                      different T7SSs, called ESX-1 to ESX-5, which are crucial
                      for growth and virulence. Here, we use a functionally
                      reconstituted ESX-5 system in the avirulent species
                      Mycobacterium smegmatis that lacks ESX-5, to define the role
                      of each esx-5 gene in system functionality. By creating an
                      array of gene deletions and assessing protein levels of
                      components and membrane complex assembly, we observed that
                      only the five components of the inner membrane complex are
                      required for its assembly. However, in addition to these
                      five core components, active secretion also depends on both
                      the Esx and PE/PPE substrates. Tagging the PPE substrates
                      followed by subcellular fractionation, surface labeling and
                      membrane extraction showed that these proteins localize to
                      the mycobacterial outer membrane. This indicates that they
                      could play a role in secretion across this enigmatic outer
                      barrier. These results provide the first full overview of
                      the role of each esx-5 gene in T7SS functionality.},
      cin          = {CSSB-UKE-TM},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / CryoMyco - Atomic dissection of
                      type VII secretion systems from pathogenic mycobacteria
                      (101030373)},
      pid          = {G:(DE-HGF)POF4-633 / G:(EU-Grant)101030373},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37747201},
      UT           = {WOS:001191361100020},
      doi          = {10.1128/msphere.00402-23},
      url          = {https://bib-pubdb1.desy.de/record/603156},
}