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@ARTICLE{Fislage:207475,
      author       = {Fislage, M. and Brosens, E. and Deyaert, E. and Spilotros,
                      Alessandro and Pardon, E. and Loris, R. and Steyaert, J. and
                      Garcia-Pino, A. and Versees, W.},
      title        = {{SAXS} {A}nalysis of the t{RNA}-{M}odifying {E}nzyme
                      {C}omplex {M}nm{E}/{M}nm{G} {R}eveals a {N}ovel
                      {I}nteraction {M}ode and {GTP}-{I}nduced {O}ligomerization},
      journal      = {Nucleic acids symposium series},
      volume       = {42},
      number       = {9},
      issn         = {1362-4962},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press8619},
      reportid     = {PUBDB-2015-01363},
      pages        = {5978 - 5992},
      year         = {2014},
      note         = {OA},
      abstract     = {Transfer ribonucleic acid (tRNA) modifications, especially
                      at the wobble position, are crucial for proper and efficient
                      protein translation. MnmE and MnmG form a protein complex
                      that is implicated in the carboxymethylaminomethyl
                      modification of wobble uridine (cmnm5U34) of certain tRNAs.
                      MnmE is a G protein activated by dimerization (GAD), and
                      active guanosine-5'-triphosphate (GTP) hydrolysis is
                      required for the tRNA modification to occur. Although
                      crystal structures of MnmE and MnmG are available, the
                      structure of the MnmE/MnmG complex (MnmEG) and the nature of
                      the nucleotide-induced conformational changes and their
                      relevance for the tRNA modification reaction remain unknown.
                      In this study, we mainly used small-angle X-ray scattering
                      to characterize these conformational changes in solution and
                      to unravel the mode of interaction between MnmE, MnmG and
                      tRNA. In the nucleotide-free state MnmE and MnmG form an
                      unanticipated asymmetric α2β2 complex. Unexpectedly, GTP
                      binding promotes further oligomerization of the MnmEG
                      complex leading to an α4β2 complex. The transition from
                      the α2β2 to the α4β2 complex is fast, reversible and
                      coupled to GTP binding and hydrolysis. We propose a model in
                      which the nucleotide-induced changes in conformation and
                      oligomerization of MnmEG form an integral part of the tRNA
                      modification reaction cycle.},
      cin          = {EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13) / PETRA Beamline P12
                      (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405 /
                      G:(DE-H253)POF2-P12-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101 / EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000336495400056},
      pubmed       = {pmid:24634441},
      doi          = {10.1093/nar/gku213},
      url          = {https://bib-pubdb1.desy.de/record/207475},
}