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@ARTICLE{Keppel:877824,
      author       = {Keppel, Marc and Hünnefeld, Max and Filipchyk, Andrei and
                      Viets, Ulrike and Davoudi, Cedric-Farhad and Krüger, Aileen
                      and Mack, Christina and Pfeifer, Eugen and Polen, Tino and
                      Baumgart, Meike and Bott, Michael and Frunzke, Julia},
      title        = {{H}rr{SA} orchestrates a systemic response to heme and
                      determines prioritization of terminal cytochrome oxidase
                      expression},
      journal      = {Nucleic acids research},
      volume       = {48},
      number       = {12},
      issn         = {0305-1048},
      address      = {London},
      publisher    = {Information Retrieval Ltd.86606},
      reportid     = {FZJ-2020-02463},
      pages        = {6547-6562},
      year         = {2020},
      note         = {Biotechnologie 1},
      abstract     = {Heme is a multifaceted molecule. While serving as a
                      prosthetic group for many important proteins, elevated
                      levels are toxic to cells. The complexity of this stimulus
                      has shaped bacterial network evolution. However, only a
                      small number of targets controlled by heme-responsive
                      regulators have been described to date. Here, we performed
                      chromatin affinity purification and sequencing to provide
                      genome-wide insights into in vivo promoter occupancy of
                      HrrA, the response regulator of the heme-regulated
                      two-component system HrrSA of Corynebacterium glutamicum.
                      Time-resolved profiling revealed dynamic binding of HrrA to
                      more than 200 different genomic targets encoding proteins
                      associated with heme biosynthesis, the respiratory chain,
                      oxidative stress response and cell envelope remodeling. By
                      repression of the extracytoplasmic function sigma factor
                      sigC, which activates the cydABCD operon, HrrA prioritizes
                      the expression of genes encoding the cytochrome bc1-aa3
                      supercomplex. This is also reflected by a significantly
                      decreased activity of the cytochrome aa3 oxidase in the
                      ΔhrrA mutant. Furthermore, our data reveal that HrrA also
                      integrates the response to heme-induced oxidative stress by
                      activating katA encoding the catalase. These data provide
                      detailed insights in the systemic strategy that bacteria
                      have evolved to respond to the versatile signaling molecule
                      heme.},
      cin          = {IBG-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581) / DFG project 284242796 -
                      Spezifität der Phosphatase-Aktivität und Interaktion
                      Häm-abhängiger Zweikomponentensysteme in Corynebacterium
                      glutamicum},
      pid          = {G:(DE-HGF)POF3-581 / G:(GEPRIS)284242796},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32453397},
      UT           = {WOS:000574288800018},
      doi          = {10.1093/nar/gkaa415},
      url          = {https://juser.fz-juelich.de/record/877824},
}