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@ARTICLE{Wolf:873824,
      author       = {Wolf, Natalie and Bussmann, Michael and Koch-Koerfges,
                      Abigail and Katcharava, Nino and Schulte, Julia and Polen,
                      Tino and Hartl, Johannes and Vorholt, Julia A. and Baumgart,
                      Meike and Bott, Michael},
      title        = {{M}olecular {B}asis of {G}rowth {I}nhibition by {A}cetate
                      of an {A}denylate {C}yclase-{D}eficient {M}utant of
                      {C}orynebacterium glutamicum},
      journal      = {Frontiers in microbiology},
      volume       = {11},
      issn         = {1664-302X},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2020-01029},
      pages        = {87},
      year         = {2020},
      note         = {Biotechnologie 1},
      abstract     = {In Corynebacterium glutamicum, cyclic adenosine
                      monophosphate (cAMP) serves as an effector of the global
                      transcriptional regulator GlxR. Synthesis of cAMP is
                      catalyzed by the membrane-bound adenylate cyclase CyaB. In
                      this study, we investigated the consequences of decreased
                      intracellular cAMP levels in a ΔcyaB mutant. While no
                      growth defect of the ΔcyaB strain was observed on glucose,
                      fructose, sucrose, or gluconate alone, the addition of
                      acetate to these growth media resulted in a severe growth
                      inhibition, which could be reversed by plasmid-based cyaB
                      expression or by supplementation of the medium with cAMP.
                      The effect was concentration- and pH-dependent, suggesting a
                      link to the uncoupling activity of acetate. In agreement,
                      the ΔcyaB mutant had an increased sensitivity to the
                      protonophore carbonyl cyanide m-chlorophenyl hydrazone
                      (CCCP). The increased uncoupler sensitivity correlated with
                      a lowered membrane potential of acetate-grown ΔcyaB cells
                      compared to wild-type cells. A reduced membrane potential
                      affects major cellular processes, such as ATP synthesis by
                      F1FO-ATP synthase and numerous transport processes. The
                      impaired membrane potential of the ΔcyaB mutant could be
                      due to a decreased expression of the cytochrome bc1-aa3
                      supercomplex, which is the major contributor of
                      proton-motive force in C. glutamicum. Expression of the
                      supercomplex genes was previously reported to be activated
                      by GlxR-cAMP. A suppressor mutant of the ΔcyaB strain with
                      improved growth on acetate was isolated, which carried a
                      single mutation in the genome leading to an Ala131Thr
                      exchange in GlxR. Introduction of this point mutation into
                      the original ΔcyaB mutant restored the growth defect on
                      acetate. This supported the importance of GlxR for the
                      phenotype of the ΔcyaB mutant and, more generally, of the
                      cAMP-GlxR system for the control of energy metabolism in C.
                      glutamicum.Introduction},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32117117},
      UT           = {WOS:000517630100001},
      doi          = {10.3389/fmicb.2020.00087},
      url          = {https://juser.fz-juelich.de/record/873824},
}