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@ARTICLE{Kallscheuer:256374,
      author       = {Kallscheuer, Nicolai and Bott, Michael and van Ooyen, Jan
                      and Polen, Tino},
      title        = {{S}ingle-{D}omain {P}eptidyl-{P}rolyl cis / trans
                      {I}somerase {F}kp{A} from {C}orynebacterium glutamicum
                      {I}mproves the {B}iomass {Y}ield at {I}ncreased {G}rowth
                      {T}emperatures},
      journal      = {Applied and environmental microbiology},
      volume       = {81},
      number       = {22},
      issn         = {1098-5336},
      address      = {Washington, DC [u.a.]},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-06331},
      pages        = {7839 - 7850},
      year         = {2015},
      note         = {Biotechnologie 1},
      abstract     = {Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the
                      rate-limiting protein folding step at peptidyl bonds
                      preceding proline residues and were found to be involved in
                      several biological processes, including gene expression,
                      signal transduction, and protein secretion. Representative
                      enzymes were found in almost all sequenced genomes,
                      including Corynebacterium glutamicum, a facultative
                      anaerobic Gram-positive and industrial workhorse for the
                      production of amino acids. In C. glutamicum, a predicted
                      single-domain FK-506 (tacrolimus) binding protein
                      (FKBP)-type PPIase (FkpA) is encoded directly downstream of
                      gltA, which encodes citrate synthase (CS). This gene cluster
                      is also present in other Actinobacteria. Here we carried out
                      in vitro and in vivo experiments to study the function and
                      influence of predicted FkpA in C. glutamicum. In vitro, FkpA
                      indeed shows typical PPIase activity with artificial
                      substrates and is inhibited by FK-506. Furthermore, FkpA
                      delays the aggregation of CS, which is also inhibited by
                      FK-506. Surprisingly, FkpA has a positive effect on the
                      activity and temperature range of CS in vitro. Deletion of
                      fkpA causes a $50\%$ reduced biomass yield compared to that
                      of the wild type when grown at 37°C, whereas there is only
                      a $10\%$ reduced biomass yield at the optimal growth
                      temperature of 30°C accompanied by accumulation of 7 mM
                      l-glutamate and 22 mM 2-oxoglutarate. Thus, FkpA may be
                      exploited for improved product formation in biotechnical
                      processes. Comparative transcriptome analysis revealed 69
                      genes which exhibit ≥2-fold mRNA level changes in C.
                      glutamicum ΔfkpA, giving insight into the transcriptional
                      response upon mild heat stress when FkpA is absent.},
      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},
      UT           = {WOS:000363463800017},
      pubmed       = {pmid:26341203},
      doi          = {10.1128/AEM.02113-15},
      url          = {https://juser.fz-juelich.de/record/256374},
}