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@ARTICLE{Fernandes:597829,
      author       = {Fernandes, Rita and Ostendorp, Anna and Ostendorp, Steffen
                      and Mehrmann, Judith and Falke, Sven and Graewert, Melissa
                      Ann and Weingartner, Magdalena and Kehr, Julia and Hoth,
                      Stefan},
      title        = {{S}tructural and functional analysis of a plant nucleolar
                      {RNA} chaperone-like protein},
      journal      = {Scientific reports},
      volume       = {13},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2023-06697},
      pages        = {9656},
      year         = {2023},
      abstract     = {Ribosome biogenesis is a key process in all eukaryotic
                      cells that requires hundreds of ribosome biogenesis factors
                      (RBFs), which are essential to build the mature ribosomes
                      consisting of proteins and rRNAs. The processing of the
                      required rRNAs has been studied extensively in yeast and
                      mammals, but in plants much is still unknown. In this study,
                      we focused on a RBF from A. thaliana that we named NUCLEOLAR
                      RNA CHAPERONE-LIKE 1 (NURC1). NURC1 was localized in the
                      nucleolus of plant cell nuclei, and other plant RBF
                      candidates shared the same localization. SEC-SAXS
                      experiments revealed that NURC1 has an elongated and
                      flexible structure. In addition, SEC-MALLS experiments
                      confirmed that NURC1 was present in its monomeric form with
                      a molecular weight of around 28 kDa. RNA binding was
                      assessed by performing microscale thermophoresis with the
                      Arabidopsis internal transcribed spacer 2 (ITS2) of the
                      polycistronic pre-rRNA precursor, which contains the 5.8S,
                      18S, and 25S rRNA. NURC1 showed binding activity to the ITS2
                      with a dissociation constant of 228 nM and exhibited RNA
                      chaperone-like activity. Our data suggested that NURC1 may
                      have a function in pre-rRNA processing and thus ribosome
                      biogenesis.},
      cin          = {EMBL / FS-CFEL-1-BMX},
      ddc          = {600},
      cid          = {I:(DE-H253)EMBL-20120731 /
                      I:(DE-H253)FS-CFEL-1-BMX-20210408},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37316549},
      UT           = {WOS:001010888200041},
      doi          = {10.1038/s41598-023-36426-4},
      url          = {https://bib-pubdb1.desy.de/record/597829},
}