The structure of the box C/D enzyme reveals regulation of RNA methylation

Post-transcriptional modifications are essential to the cell life cycle, as they affect both pre-ribosomal RNA processing and ribosome assembly. The box C/D ribonucleoprotein enzyme that methylates ribosomal RNA at the 2′-O-ribose uses a multitude of guide RNAs as templates for the recognition of rR...

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Autori principali: Lapinaitė, Audronė (Autore) , Simon, Bernd (Autore) , Skjaerven, Lars (Autore) , Rakwalska-Bange, Magdalena (Autore) , Gabel, Frank (Autore) , Carlomagno, Teresa (Autore)
Natura: Article (Journal)
Lingua:inglese
Pubblicazione: 13 October 2013
In: Nature
Year: 2013, Volume: 502, Pages: 519-523
ISSN:1476-4687
DOI:10.1038/nature12581
Accesso online:Verlag, Volltext: https://doi.org/10.1038/nature12581
Verlag, Volltext: https://www.nature.com/articles/nature12581
Testo
Note sull'autore:Audrone Lapinaite, Bernd Simon, Lars Skjaerven, Magdalena Rakwalska-Bange, Frank Gabel & Teresa Carlomagno
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Riassunto:Post-transcriptional modifications are essential to the cell life cycle, as they affect both pre-ribosomal RNA processing and ribosome assembly. The box C/D ribonucleoprotein enzyme that methylates ribosomal RNA at the 2′-O-ribose uses a multitude of guide RNAs as templates for the recognition of rRNA target sites. Two methylation guide sequences are combined on each guide RNA, the significance of which has remained unclear. Here we use a powerful combination of NMR spectroscopy and small-angle neutron scattering to solve the structure of the 390 kDa archaeal RNP enzyme bound to substrate RNA. We show that the two methylation guide sequences are located in different environments in the complex and that the methylation of physiological substrates targeted by the same guide RNA occurs sequentially. This structure provides a means for differential control of methylation levels at the two sites and at the same time offers an unexpected regulatory mechanism for rRNA folding.
Descrizione del documento:Gesehen am 12.10.2021
Descrizione fisica:Online Resource
ISSN:1476-4687
DOI:10.1038/nature12581