% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Genna:820513,
      author       = {Genna, Vito and Gaspari, Roberto and Dal Peraro, Matteo
                      and De Vivo, Marco},
      title        = {{C}ooperative motion of a key positively charged residue
                      and metal ions for {DNA} replication catalyzed by human
                      {DNA} {P}olymerase-η},
      journal      = {Nucleic acids symposium series},
      volume       = {44},
      number       = {6},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press69994},
      reportid     = {FZJ-2016-05806},
      pages        = {2827 - 2836},
      year         = {2016},
      abstract     = {Trans-lesion synthesis polymerases, like DNA Polymerase-η
                      (Pol-η), are essential for cell survival. Pol-η bypasses
                      ultraviolet-induced DNA damages via a two-metal-ion
                      mechanism that assures DNA strand elongation, with formation
                      of the leaving group pyrophosphate (PPi). Recent structural
                      and kinetics studies have shown that Pol-η function depends
                      on the highly flexible and conserved Arg61 and,
                      intriguingly, on a transient third ion resolved at the
                      catalytic site, as lately observed in other nucleic
                      acid-processing metalloenzymes. How these conserved
                      structural features facilitate DNA replication, however, is
                      still poorly understood. Through extended molecular dynamics
                      and free energy simulations, we unravel a highly cooperative
                      and dynamic mechanism for DNA elongation and repair, which
                      is here described by an equilibrium ensemble of structures
                      that connect the reactants to the products in Pol-η
                      catalysis. We reveal that specific conformations of Arg61
                      help facilitate the recruitment of the incoming base and
                      favor the proper formation of a pre-reactive complex in
                      Pol-η for efficient DNA editing. Also, we show that a third
                      transient metal ion, which acts concertedly with Arg61,
                      serves as an exit shuttle for the leaving PPi. Finally, we
                      discuss how this effective and cooperative mechanism for DNA
                      repair may be shared by other DNA-repairing polymerases.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000374570500036},
      pubmed       = {pmid:26935581},
      doi          = {10.1093/nar/gkw128},
      url          = {https://juser.fz-juelich.de/record/820513},
}