title: Prefabrication of a ribosomal protein subcomplex essential for eukaryotic ribosome formation.
abstract: Spatial clustering of ribosomal proteins (r-proteins) through tertiary interactions is a striking structural feature of the eukaryotic ribosome. However, the functional importance of these intricate inter-connections, and how they are established is currently unclear. Here, we reveal that a conserved ATPase, Fap7, organizes interactions between neighboring r-proteins uS11 and eS26 prior to their delivery to the earliest ribosome precursor, the 90S. In vitro, uS11 only when bound to Fap7 becomes competent to recruit eS26 through tertiary contacts found between these r-proteins on the mature ribosome. Subsequently, Fap7 ATPase activity unloads the uS11:eS26 subcomplex onto its rRNA binding site, and therefore ensures stoichiometric integration of these r-proteins into the 90S. Fap7-depletion in vivo renders uS11 susceptible to proteolysis, and precludes eS26 incorporation into the 90S. Thus, prefabrication of a native-like r-protein subcomplex drives efficient and accurate construction of the eukaryotic ribosome.
authors.affiliation: Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.|Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
authors.forename: Cohue
authors.initials: C
authors.lastname: Peña
authors.affiliation: Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
authors.forename: Sabina
authors.initials: S
authors.lastname: Schütz
authors.affiliation: Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
authors.forename: Ute
authors.initials: U
authors.lastname: Fischer
authors.affiliation: Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
authors.forename: Yiming
authors.initials: Y
authors.lastname: Chang
authors.affiliation: Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
authors.forename: Vikram G
authors.identifier: 0000-0001-7950-5746
authors.initials: VG
authors.lastname: Panse
mesh_terms: D000263:Adenylate Kinase / Q000378:metabolism*; D046911:Macromolecular Substances / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D043583:Nucleoside-Triphosphatase / Q000378:metabolism*; D055503:Protein Multimerization; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D046911:Macromolecular Substances; D009687:Nuclear Proteins; C489204:RPS26A protein, S cerevisiae; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; C045454:ribosomal protein S11; D000263:Adenylate Kinase; C406456:FAP7 protein, S cerevisiae; D043583:Nucleoside-Triphosphatase
keywords: ATPases; Fap7; S. cerevisiae; Tsr2; biochemistry; eukaryotic ribosomal proteins; protein complexes; ribosome assembly