Analysis of the interactome of ribosomal protein S19 mutants

Marianna Caterino, Anna Aspesi, Elisa Pavesi, Esther Imperlini, Daniela Pagnozzi, Laura Ingenito, Claudio Santoro, Irma Dianzani, Margherita Ruoppolo

Research output: Contribution to journalArticlepeer-review

Abstract

Diamond-Blackfan anemia, characterized by defective erythroid progenitor maturation, is caused in one-fourth of cases by mutations of ribosomal protein S19 (RPS19), which is a component of the ribosomal 40S subunit. Our previous work described proteins interacting with RPS19 with the aim to determine its functions. Here, two RPS19 mutants, R62W and R101H, have been selected to compare their interactomes versus the wild-type protein one, using the same functional proteomic approach that we employed to characterize RPS19 interactome. Mutations R62W and R101H impair RPS19 ability to associate with the ribosome. Results presented in this paper highlight the striking differences between the interactomes of wild-type and mutant RPS19 proteins. In particular, mutations abolish interactions with proteins having splicing, translational and helicase activity, thus confirming the role of RPS19 in RNA processing/metabolism and translational control.

Original languageEnglish
Pages (from-to)2286-2296
Number of pages11
JournalProteomics
Volume14
Issue number20
DOIs
Publication statusPublished - Oct 1 2014

Keywords

  • Diamond-Blackfan anemia
  • Protein-protein interaction in ribosome
  • Ribosomal assembly
  • Ribosomal function
  • Ribosomal proteins
  • Systems biology

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Medicine(all)

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