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@ARTICLE{Caruso:842938,
      author       = {Caruso, Icaro P. and Panwalkar, Vineet and Coronado, Monika
                      A. and Dingley, Andrew and Cornelio, Marinonio L. and
                      Willbold, Dieter and Arni, Raghuvir K. and Eberle, Raphael
                      J.},
      title        = {{S}tructure and interaction of {C}orynebacterium
                      pseudotuberculosis cold shock protein {A} with {Y}-box
                      single-stranded {DNA} fragment.},
      journal      = {EJB},
      volume       = {285},
      number       = {2},
      issn         = {0014-2956},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2018-01101},
      pages        = {372-390},
      year         = {2018},
      abstract     = {Cold shock proteins (Csps) function to preserve cell
                      viability at low tem-peratures by binding to nucleic acids
                      and consequently control gene expres-sion. The mesophilic
                      bacterium Corynebacterium pseudotuberculosis is thecausative
                      agent of caseous lymphadenitis in animals, and infection in
                      live-stock is a considerable economic burden worldwide. In
                      this report, thestructure of cold shock protein A from Cp (
                      Cp-CspA) and biochemicalanalysis of its
                      temperature-dependent interaction with a Y-box ssDNAmotif is
                      presented. The Cp-CspA structure contains five b-strands
                      makingup a b-barrel fold with 11 hydrophobic core residues
                      and two salt bridgesthat confers it with a melting
                      temperature of ~ 54 °C that is similar tomesophilic
                      Bs-CspB. Chemical shift perturbations analysis revealed
                      thatresidues in the nucleic acid-binding motifs (RNP 1 and
                      2) and loop 3 areinvolved in binding to the Y-box fragment
                      either by direct interaction orby conformational
                      rearrangements remote from the binding region. Fluo-rescence
                      quenching experiments of Cp-CspA showed that the
                      dissociationconstants for Y-box ssDNA binding is nanomolar
                      and the binding affinitydecreased as the temperature
                      increased, indicating that the interaction isenthalpically
                      driven and the hydrogen bonds and van der Waals forces
                      areimportant contributions for complex stabilization. The
                      Y31 of Cp-CspA isa particular occurrence among Csps from
                      mesophilic bacteria that providea possible explanation for
                      the higher binding affinity to ssDNA than thatobserved for
                      Bs-CspB. Anisotropy measurements indicated that the
                      reduc-tion in molecular mobility of Cp-CspA upon Y-box
                      binding is character-ized by a cooperative process.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29197185},
      UT           = {WOS:000423416700012},
      doi          = {10.1111/febs.14350},
      url          = {https://juser.fz-juelich.de/record/842938},
}