Functional organization of box C/D RNA-guided RNA methyltransferase

Zuxiao Yang, Jiayin Wang, Lin Huang, David M. J. Lilley, Keqiong Ye (Lead / Corresponding author)

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Abstract

Box C/D RNA protein complexes (RNPs) catalyze site-specific 2'-O-methylation of RNA with specificity determined by guide RNAs. In eukaryotic C/D RNP, the paralogous Nop58 and Nop56 proteins specifically associate with terminal C/D and internal C'/D' motifs of guide RNAs, respectively. We have reconstituted active C/D RNPs with recombinant proteins of the thermophilic yeast Chaetomium thermophilum. Nop58 and Nop56 could not distinguish between the two C/D motifs in the reconstituted enzyme, suggesting that the assembly specificity is imposed by trans-acting factors in vivo. The two C/D motifs are functionally independent and halfmer C/D RNAs can also guide site-specific methylation. Extensive pairing between C/D RNA and substrate is inhibitory to modification for both yeast and archaeal C/D RNPs. N6-methylated adenine at box D/D' interferes with the function of the coupled guide. Our data show that all C/D RNPs share the same functional organization and mechanism of action and provide insight into the assembly specificity of eukaryotic C/D RNPs.

Original languageEnglish
Pages (from-to)5094-5105
Number of pages12
JournalNucleic Acids Research
Volume48
Issue number9
Early online date16 Apr 2020
DOIs
Publication statusPublished - 21 May 2020

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