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@ARTICLE{Li:888536,
      author       = {Li, Yuan and Mohanty, Sandipan and Nilsson, Daniel and
                      Hansson, Bengt and Mao, Kangshan and Irbäck, Anders},
      title        = {{W}hen a foreign gene meets its native counterpart:
                      computational biophysics analysis of two {P}gi{C} loci in
                      the grass {F}estuca ovina},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-05000},
      pages        = {18752},
      year         = {2020},
      abstract     = {Duplicative horizontal gene transfer may bring two
                      previously separated homologous genes together, which may
                      raise questions about the interplay between the gene
                      products. One such gene pair is the “native” PgiC1 and
                      “foreign” PgiC2 in the perennial grass Festuca ovina.
                      Both PgiC1 and PgiC2 encode cytosolic phosphoglucose
                      isomerase, a dimeric enzyme whose proper binding is
                      functionally essential. Here, we use biophysical simulations
                      to explore the inter-monomer binding of the two homodimers
                      and the heterodimer that can be produced by PgiC1 and PgiC2
                      in F. ovina. Using simulated native-state ensembles, we
                      examine the structural properties and binding tightness of
                      the dimers. In addition, we investigate their ability to
                      withstand dissociation when pulled by a force. Our results
                      suggest that the inter-monomer binding is tighter in the
                      PgiC2 than the PgiC1 homodimer, which could explain the more
                      frequent occurrence of the foreign PgiC2 homodimer in dry
                      habitats. We further find that the PgiC1 and PgiC2 monomers
                      are compatible with heterodimer formation; the computed
                      binding tightness is comparable to that of the PgiC1
                      homodimer. Enhanced homodimer stability and capability of
                      heterodimer formation with PgiC1 are properties of PgiC2
                      that may contribute to the retaining of the otherwise
                      redundant PgiC2 gene.},
      cin          = {JSC},
      ddc          = {600},
      cid          = {I:(DE-Juel1)JSC-20090406},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33127989},
      UT           = {WOS:000591917600027},
      doi          = {10.1038/s41598-020-75650-0},
      url          = {https://juser.fz-juelich.de/record/888536},
}