<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Fernández-Pevida, Antonio</dc:creator>
  <dc:creator>Martín-Villanueva, Sara</dc:creator>
  <dc:creator>Murat, Guillaume</dc:creator>
  <dc:creator>Lacombe, Thierry</dc:creator>
  <dc:creator>Kressler, Dieter</dc:creator>
  <dc:creator>Cruz, Jesús de la</dc:creator>
  <dc:date>2016-09-19</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">The archaea-/eukaryote-specific 40S-ribosomal-subunit protein S31 is expressed as  an ubiquitin fusion protein in eukaryotes and consists of a conserved body and a  eukaryote-specific N-terminal extension. In yeast, S31 is a practically essential protein,  which is required for cytoplasmic 20S pre-rRNA maturation. Here, we have studied the  role of the N-terminal extension of the yeast S31 protein. We show that deletion of this  extension partially impairs cell growth and 40S subunit biogenesis and confers  hypersensitivity to aminoglycoside antibiotics. Moreover, the extension harbours a  nuclear localization signal that promotes active nuclear import of S31, which  associates with pre-ribosomal particles in the nucleus. In the absence of the extension,  truncated S31 inefficiently assembles into pre-40S particles and two subpopulations of  mature small subunits, one lacking and another one containing truncated S31, can be  identified. Plasmid-driven overexpression of truncated S31 partially suppresses the  growth and ribosome biogenesis defects but, conversely, slightly enhances the  hypersensitivity to aminoglycosides. Altogether, these results indicate that the N- terminal extension facilitates the assembly of S31 into pre-40S particles and  contributes to the optimal translational activity of mature 40S subunits but has only a  minor role in cytoplasmic cleavage of 20S pre-rRNA at site D.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/unifr/documents/305354</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305354/files/kre_esn.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkw641</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Nucleic Acids Research. - 2016, vol. 44, no. 16, p. 7777–7791</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
