Publication Date:
2013-10-15
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lapinaite, Audrone -- Simon, Bernd -- Skjaerven, Lars -- Rakwalska-Bange, Magdalena -- Gabel, Frank -- Carlomagno, Teresa -- England -- Nature. 2013 Oct 24;502(7472):519-23. doi: 10.1038/nature12581. Epub 2013 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24121435" target="_blank"〉PubMed〈/a〉
Keywords:
Apoproteins/chemistry/metabolism
;
Archaeal Proteins/chemistry/metabolism
;
Biocatalysis
;
Chromosomal Proteins, Non-Histone/metabolism
;
Methylation
;
Models, Molecular
;
Multiprotein Complexes/chemistry/metabolism
;
Nucleic Acid Conformation
;
Pyrococcus furiosus/*enzymology/*genetics
;
RNA Folding
;
*RNA Processing, Post-Transcriptional
;
RNA, Archaeal/chemistry/genetics/metabolism
;
RNA, Guide/chemistry/genetics/metabolism
;
RNA, Ribosomal/*chemistry/*metabolism
;
Ribonucleoproteins, Small Nucleolar/*chemistry/*metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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