Journal article

The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits

  • Fernández-Pevida, Antonio Instituto de Biomedicina de Sevilla (IBiS), Universidad de Sevilla, Spain - Departamento de Genetica, Universidad de Sevilla, Spain
  • Martín-Villanueva, Sara Instituto de Biomedicina de Sevilla (IBiS), Universidad de Sevilla, Spain - Departamento de Genetica, Universidad de Sevilla, Spain
  • Murat, Guillaume Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland and
  • Lacombe, Thierry Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland
  • Kressler, Dieter Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland and
  • Cruz, Jesús de la Instituto de Biomedicina de Sevilla (IBiS), Universidad de Sevilla, Spain - Departamento de Genetica, Universidad de Sevilla, Spain
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    19.09.2016
Published in:
  • Nucleic Acids Research. - 2016, vol. 44, no. 16, p. 7777–7791
English 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.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biology
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/305354
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