期刊
NUCLEUS-AUSTIN
卷 2, 期 1, 页码 30-37出版社
LANDES BIOSCIENCE
DOI: 10.4161/nucl.2.1.14437
关键词
nucleolus; SUMO; Nop5/Nop58; snoRNA; snoRNP; SILAC
类别
资金
- Wellcome Trust [083524/Z/07/Z]
- MRC [69159]
- UK RASOR network
- EU network EURASNET [LSHG-CT-2005-518238]
- EU network PROSPECTS [HEALTH-F4-2008-201648]
- Medical Research Council [G0301131] Funding Source: researchfish
- MRC [G0301131] Funding Source: UKRI
A role for SUMOylation in the biogenesis and/or function of Box C/D snoRNPs has been reported, mediated via SUMO2 conjugation to the core snoRNP protein, Nop58. A quantitative proteomics screen, based on SILAC (stable-isotope labeling by amino acids in cell culture) and mass spectrometry using extracts prepared from cultured mammalian cells expressing either 6His-SUMO1 or -SUMO2, revealed that the snoRNP-related proteins Nop58, Nhp2, DKC1 and NOLC1 are amongst the main SUMO-modified proteins in the nucleolus. SUMOylation of Nhp2 and endogenous Nop58 was confirmed using a combination of in vitro and cell-based assays and the modified lysines identified by site-directed mutagenesis. SUMOylation of Nop58 was found to be important for high-affinity Box C/D snoRNA binding and the localization of newly transcribed snoRNAs to the nucleolus. Here, these findings are reviewed and a model for understanding Nop58 SUMOylation in the context of Box C/D snoRNP biogenesis is presented. Given the essential role of snoRNPs in the modification of pre-ribosomal RNA, this work suggests that SUMO, snoRNPs and ribosome assembly, and thus cellular translation, growth and proliferation, may be linked via novel mechanisms which warrant further investigation.
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