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@ARTICLE{Bott:1010606,
      author       = {Bott, Michael and Sundermeyer, Lea and Folkerts, Jan-Gerrit
                      and Lückel, Benita and Mack, Christina and Baumgart, Meike},
      title        = {{C}ellular localization of the hybrid
                      pyruvate/2-oxoglutarate dehydrogenase complex in the
                      actinobacterium {C}orynebacterium glutamicum},
      journal      = {Microbiology spectrum},
      volume       = {11},
      number       = {5},
      issn         = {2165-0497},
      address      = {Birmingham, Ala.},
      publisher    = {ASM},
      reportid     = {FZJ-2023-03125},
      pages        = {1-17},
      year         = {2023},
      abstract     = {For many bacterial proteins, specific localizations within
                      the cell have been demonstrated, but enzymes involved in
                      central metabolism are usually considered to be homogenously
                      distributed within the cytoplasm. Here, we provide an
                      example for a spatially defined localization of a unique
                      enzyme complex found in actinobacteria, the hybrid
                      pyruvate/2-oxoglutarate dehydrogenase complex (PDH-ODH). In
                      non-actinobacterial cells, PDH and ODH form separate
                      multienzyme complexes of megadalton size composed of three
                      different subunits, E1, E2, and E3. The actinobacterial
                      PDH-ODH complex is composed of four subunits, AceE (E1p),
                      AceF (E2p), Lpd (E3), and OdhA (E1oE2o). Using fluorescence
                      microscopy, we observed that in Corynebacterium glutamicum,
                      all four subunits are co-localized in distinct spots at the
                      cell poles, and in larger cells, additional spots are
                      present at mid-cell. These results further confirm the
                      existence of the hybrid complex. The unphosporylated OdhI
                      protein, which binds to OdhA and inhibits ODH activity, was
                      co-localized with OdhA at the poles, whereas phosphorylated
                      OdhI, which does not bind OdhA, was distributed in the
                      entire cytoplasm. Isocitrate dehydrogenase and glutamate
                      dehydrogenase, both metabolically linked to ODH, were evenly
                      distributed in the cytoplasm. Based on the available
                      structural data for individual PDH-ODH subunits, a novel
                      supramolecular architecture of the hybrid complex differing
                      from classical PDH and ODH complexes has to be postulated.
                      Our results suggest that localization at the poles or at
                      mid-cell is most likely caused by nucleoid exclusion and
                      results in a spatially organized metabolism in
                      actinobacteria, with consequences yet to be studied.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37754766},
      UT           = {WOS:001074023400001},
      doi          = {10.1128/spectrum.02668-23},
      url          = {https://juser.fz-juelich.de/record/1010606},
}