A dimeric structure for archaeal box C/D small ribonucleoproteins

Franziska Bleichen, Keith T. Gagnon, Bernard A. Brown, E. Stuart Maxwell, Andres E. Leschziner, Vinzenz M. Unger, Susan J. Baserga

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

Methylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2-0ribose 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 singleparticle 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.

Original languageEnglish (US)
Pages (from-to)1384-1387
Number of pages4
JournalScience
Volume325
Issue number5946
DOIs
StatePublished - 2009

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A dimeric structure for archaeal box C/D small ribonucleoproteins'. Together they form a unique fingerprint.

Cite this