Analysis of the interactome of ribosomal protein S19 mutants.

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. The data have been deposited to the ProteomeXchange with identifier PXD000640 (http://proteomecentral.proteomexchange.org/dataset/PXD000640).

• Authors: Marianna Caterino, Anna Aspesi, Elisa Pavesi, Esther Imperlini, Daniela Pagnozzi, Laura Ingenito, Claudio Santoro, Irma Dianzani, Margherita Ruoppolo
• Journal: Proteomics (Proteomics) Vol. 14 Issue 20 Pg. 2286-96 (Oct 2014) ISSN: 1615-9861 [Electronic] Germany
• PMID: 25069755 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Chemical References

• Ribosomal Proteins
• ribosomal protein S19

Topics

• Anemia, Diamond-Blackfan (genetics, metabolism)
• Humans
• Point Mutation
• Protein Interaction Mapping (methods)
• Protein Interaction Maps
• Proteomics (methods)
• Ribosomal Proteins (genetics, metabolism)
• Ribosomes (genetics, metabolism)
• Systems Biology (methods)