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

Risultato della ricerca: Contributo su rivistaArticolo in rivistapeer 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.

Lingua originaleInglese
pagine (da-a)2286-2296
Numero di pagine11
RivistaProteomics
Volume14
Numero di pubblicazione20
DOI
Stato di pubblicazionePubblicato - 1 ott 2014

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