% 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{Wald:486215,
      author       = {Wald, Jiri and Fahrenkamp, Dirk and Goessweiner-Mohr,
                      Nikolaus and Lugmayr, Wolfgang and Ciccarelli, Luciano and
                      Vesper, Oliver and Marlovits, Thomas},
      title        = {{M}echanism of {AAA}+ {ATP}ase-mediated
                      {R}uv{AB}–{H}olliday junction branch migration},
      journal      = {Nature},
      volume       = {609},
      number       = {7927},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2022-07157},
      pages        = {630 - 639},
      year         = {2022},
      abstract     = {The Holliday junction is a key intermediate formed during
                      DNA recombination across all kingdoms of life1. In bacteria,
                      the Holliday junction is processed by two homo-hexameric
                      AAA+ ATPase RuvB motors, which assemble together with the
                      RuvA–Holliday junction complex to energize the
                      strand-exchange reaction2. Despite its importance for
                      chromosome maintenance, the structure and mechanism by which
                      this complex facilitates branch migration are unknown. Here,
                      using time-resolved cryo-electron microscopy, we obtained
                      structures of the ATP-hydrolysing RuvAB complex in seven
                      distinct conformational states, captured during assembly and
                      processing of a Holliday junction. Five structures together
                      resolve the complete nucleotide cycle and reveal the
                      spatiotemporal relationship between ATP hydrolysis,
                      nucleotide exchange and context-specific conformational
                      changes in RuvB. Coordinated motions in a converter formed
                      by DNA-disengaged RuvB subunits stimulate hydrolysis and
                      nucleotide exchange. Immobilization of the converter enables
                      RuvB to convert the ATP-contained energy into a lever
                      motion, which generates the pulling force driving the branch
                      migration. We show that RuvB motors rotate together with the
                      DNA substrate, which, together with a progressing nucleotide
                      cycle, forms the mechanistic basis for DNA recombination by
                      continuous branch migration. Together, our data decipher the
                      molecular principles of homologous recombination by the
                      RuvAB complex, elucidate discrete and sequential
                      transition-state intermediates for chemo-mechanical coupling
                      of hexameric AAA+ motors and provide a blueprint for the
                      design of state-specific compounds targeting AAA+ motors.},
      cin          = {FS-CS / CSSB-UKE-TM},
      ddc          = {500},
      cid          = {I:(DE-H253)FS-CS-20210408 /
                      I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36002576},
      UT           = {WOS:000844487700001},
      doi          = {10.1038/s41586-022-05121-1},
      url          = {https://bib-pubdb1.desy.de/record/486215},
}