Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control - Inria - Institut national de recherche en sciences et technologies du numérique Accéder directement au contenu
Article Dans Une Revue Journal of Cell Biology Année : 2014

Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control

Résumé

In vitro, assembly of box C/D small nucleolar ribonucleoproteins (snoRNPs) involves the sequential recruitment of core proteins to snoRNAs. In vivo, however, assembly factors are required (NUFIP, BCD1, and the FISP90-R2TP complex), and it is unknown whether a similar sequential scheme applies. In this paper, we describe systematic quantitative stable isotope labeling by amino acids in cell culture proteomic experiments and the crystal structure of the core protein Snu 13p/15.5K bound to a fragment of the assembly factor Rsa1p/NUFIP. This revealed several unexpected features: (a) the existence of a protein-only pre-snoRNP complex containing five assembly factors and two core proteins, 15.5K and Nop58; (b) the characterization of ZNHIT3, which is present in the protein-only complex but gets released upon binding to C/D snoRNAs; (c) the dynamics of the R2TP complex, which,appears a to load/unload RuvBL AAA(+) adenosine triphosphatase from pre-snoRNPs; and (d) a potential mechanism for preventing premature activation of snoRNP catalytic activity. These data provide a framework for understanding the assembly of box C/D snoRNPs.
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hal-01453204 , version 1 (28-05-2021)

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Jonathan Bizarro, Christophe Charron, Séverine Boulon, Belinda Westman, Bérengère Pradet-Balade, et al.. Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control. Journal of Cell Biology, 2014, 207 (4), pp.463-480. ⟨10.1083/jcb.201404160⟩. ⟨hal-01453204⟩
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