Journal article
Human ribosomes from cells with reduced dyskerin levels are intrinsically altered in translation
M Penzo, L Rocchi, S Brugiere, D Carnicelli, C Onofrillo, Y Coute, M Brigotti, L Montanaro
FASEB Journal | FEDERATION AMER SOC EXP BIOL | Published : 2015
DOI: 10.1096/fj.15-270991
Abstract
Dyskerin is a pseudouridine (Ψ) synthase involved in fundamental cellular processes including uridine modification in rRNA and small nuclear RNA and telomere stabilization. Dyskerin functions are altered in X-linked dyskeratosis congenita (X-DC) and cancer. Dyskerin's role in rRNA pseudouridylation has been suggested to underlie the alterations in mRNA translation described in cells lacking dyskerin function, although relevant direct evidences are currently lacking. Our purpose was to establish definitely whether defective dyskerin function might determine an intrinsic ribosomal defect leading to an altered synthetic activity. Therefore, ribosomes from dyskerin-depleted human cells were puri..
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Awarded by Association for International Cancer Research
Funding Acknowledgements
The authors are in debt to Drs. D. Ruggero, B. Mazumder and J.-J. Diaz for providing reagents, and to Drs. O. Gandrillon, S. Giraud, A. T. Thu Lefebvre, and L. Grossier (Centre de Genetique et de Physiologie Moleculaire et Cellulaire, Lyon, France) for help in the preliminary part of the study and for discussion. The authors thank the Center for Applied Biomedical Research of S. Orsola-Malpighi University Hospital in Bologna for making available several instruments. This work has been supported by grants from the Association for International Cancer Research (09-0083), Associazione Italiana per la Ricerca sul Cancro (IG-11416), the Italian Ministry of Education, University and National Research Project (Grant 20104AE23N_002), the PRIME-XS project (Grant 262067), funded by the European Union 7th Framework Programme (awarded to L.M.), and Funds from the Pallotti Legacy for research on cancer (to L.M. and M.B.). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (http://proteomecentral.proteomexchange.org) via the PRIDE partner repository (31) with the data set identifier PXD001274.