PLoS ONE (Jan 2013)

Studies on the assembly characteristics of large subunit ribosomal proteins in S. cerevisae.

  • Uli Ohmayer,
  • Michael Gamalinda,
  • Martina Sauert,
  • Julius Ossowski,
  • Gisela Pöll,
  • Jan Linnemann,
  • Thomas Hierlmeier,
  • Jorge Perez-Fernandez,
  • Beril Kumcuoglu,
  • Isabelle Leger-Silvestre,
  • Marlène Faubladier,
  • Joachim Griesenbeck,
  • John Woolford,
  • Herbert Tschochner,
  • Philipp Milkereit

DOI
https://doi.org/10.1371/journal.pone.0068412
Journal volume & issue
Vol. 8, no. 7
p. e68412

Abstract

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During the assembly process of ribosomal subunits, their structural components, the ribosomal RNAs (rRNAs) and the ribosomal proteins (r-proteins) have to join together in a highly dynamic and defined manner to enable the efficient formation of functional ribosomes. In this work, the assembly of large ribosomal subunit (LSU) r-proteins from the eukaryote S. cerevisiae was systematically investigated. Groups of LSU r-proteins with specific assembly characteristics were detected by comparing the protein composition of affinity purified early, middle, late or mature LSU (precursor) particles by semi-quantitative mass spectrometry. The impact of yeast LSU r-proteins rpL25, rpL2, rpL43, and rpL21 on the composition of intermediate to late nuclear LSU precursors was analyzed in more detail. Effects of these proteins on the assembly states of other r-proteins and on the transient LSU precursor association of several ribosome biogenesis factors, including Nog2, Rsa4 and Nop53, are discussed.