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TitleA dimeric structure for archaeal box C/D small ribonucleoproteins.
Journal, issue, pagesScience, Vol. 325, Issue 5946, Page 1384-1387, Year 2009
Publish dateSep 11, 2009
AuthorsFranziska Bleichert / Keith T Gagnon / Bernard A Brown / E Stuart Maxwell / Andres E Leschziner / Vinzenz M Unger / Susan J Baserga /
PubMed AbstractMethylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2'-O-ribose methylations are carried out by box C/D guide ribonucleoproteins [small ribonucleoproteins (sRNPs) ...Methylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2'-O-ribose methylations are carried out by box C/D guide ribonucleoproteins [small ribonucleoproteins (sRNPs) and small nucleolar ribonucleoproteins (snoRNPs)], which are conserved from archaea to eukaryotes. Methylation is dictated by base pairing between the specific guide RNA component of the sRNP or snoRNP and the target rRNA. We determined the structure of a reconstituted and catalytically active box C/D sRNP from the archaeon Methanocaldococcus jannaschii by single-particle electron microscopy. We found that archaeal box C/D sRNPs unexpectedly formed a dimeric structure with an alternative organization of their RNA and protein components that challenges the conventional view of their architecture. Mutational analysis demonstrated that this di-sRNP structure was relevant for the enzymatic function of archaeal box C/D sRNPs.
External linksScience / PubMed:19745151 / PubMed Central
MethodsEM (single particle)
Resolution27.0 Å
Structure data

EMDB-1636:
A dimeric structure for archaeal methylation-guide small ribonucleoproteins
Method: EM (single particle) / Resolution: 27.0 Å

Source
  • Methanocaldococcus jannaschii (archaea)

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