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@ARTICLE{Kever:897245,
      author       = {Kever, Larissa and Hünnefeld, Max and Brehm, Jannis and
                      Heermann, Ralf and Frunzke, Julia},
      title        = {{I}dentification of {G}ip as a novel phage‐encoded gyrase
                      inhibitor protein of {C}orynebacterium glutamicum},
      journal      = {Molecular microbiology},
      volume       = {116},
      number       = {5},
      issn         = {1365-2958},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2021-03707},
      pages        = {1268 - 1280},
      year         = {2021},
      note         = {Biotechnologie 1},
      abstract     = {By targeting key regulatory hubs of their host,
                      bacteriophages represent a powerful source for the
                      identification of novel antimicrobial proteins. Here, a
                      screening of small cytoplasmic proteins encoded by the CGP3
                      prophage of Corynebacterium glutamicum resulted in the
                      identification of the gyrase-inhibiting protein Cg1978,
                      termed Gip. Pull-down assays and surface plasmon resonance
                      revealed a direct interaction of Gip with the gyrase subunit
                      A (GyrA). The inhibitory activity of Gip was shown to be
                      specific to the DNA gyrase of its bacterial host C.
                      glutamicum. Overproduction of Gip in C. glutamicum resulted
                      in a severe growth defect as well as an induction of the SOS
                      response. Furthermore, reporter assays revealed an
                      RecA-independent induction of the cryptic CGP3 prophage,
                      most likely caused by topological alterations.
                      Overexpression of gip was counteracted by an increased
                      expression of gyrAB and a reduction of topA expression at
                      the same time, reflecting the homeostatic control of DNA
                      topology. We postulate that the prophage-encoded Gip protein
                      plays a role in modulating gyrase activity to enable
                      efficient phage DNA replication. A detailed elucidation of
                      the mechanism of action will provide novel directions for
                      the design of drugs targeting DNA gyrase.},
      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       = {pmid:34536319},
      UT           = {WOS:000701241500001},
      doi          = {10.1111/mmi.14813},
      url          = {https://juser.fz-juelich.de/record/897245},
}