Abstract
Methylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2′‐O‐ribose methylations are carried out by small (nucleolar) box C/D guide ribonucleoproteins (s(no)RNPs), which are ubiquitous in nature from archaea to eukaryotes. Each site of methylation is dictated by base pairing between the specific guide s(no)RNA component of the s(no)RNP and the target rRNA. We have determined the first structure of a reconstituted and catalytically active box C/D sRNP by electron microscopy and single particle analysis. Our results reveal that archaeal box C/D sRNPs form an unexpected di‐sRNP structure which is required for efficient methylation activity, challenging the conventional paradigm of box C/D s(no)RNP architecture.This work was supported by the NIH and the Boehringer Ingelheim Fonds.
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