+Search query
-Structure paper
Title | Box C/D sRNA stem ends act as stabilizing anchors for box C/D di-sRNPs. |
---|---|
Journal, issue, pages | Nucleic Acids Res, Vol. 44, Issue 18, Page 8976-8989, Year 2016 |
Publish date | Oct 14, 2016 |
Authors | W S Vincent Yip / Hideki Shigematsu / David W Taylor / Susan J Baserga / |
PubMed Abstract | Ribosomal RNA (rRNA) modifications are essential for ribosome function in all cellular organisms. Box C/D small (nucleolar) ribonucleoproteins [s(no)RNPs] catalyze 2'-O-methylation, one rRNA ...Ribosomal RNA (rRNA) modifications are essential for ribosome function in all cellular organisms. Box C/D small (nucleolar) ribonucleoproteins [s(no)RNPs] catalyze 2'-O-methylation, one rRNA modification type in Eukarya and Archaea. Negatively stained electron microscopy (EM) models of archaeal box C/D sRNPs have demonstrated the dimeric sRNP (di-sRNP) architecture, which has been corroborated by nuclear magnetic resonance (NMR) studies. Due to limitations of the structural techniques, the orientation of the box C/D sRNAs has remained unclear. Here, we have used cryo-EM to elucidate the sRNA orientation in a M. jannaschii box C/D di-sRNP. The cryo-EM reconstruction suggests a parallel orientation of the two sRNAs. Biochemical and structural analyses of sRNPs assembled with mutant sRNAs indicate a potential interaction between the sRNA stem ends. Our results suggest that the parallel arrangement of the sRNAs juxtaposes their stem ends into close proximity to allow for a stabilizing interaction that helps maintain the di-sRNP architecture. |
External links | Nucleic Acids Res / PubMed:27342279 / PubMed Central |
Methods | EM (single particle) |
Resolution | 9.0 Å |
Structure data | EMDB-8146: |
Source |
|