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The box C/D sRNP dimeric architecture is conserved across domain Archaea
Kathleen R Bower-Phipps1, David W Taylor, Hong-Wei Wang
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
RNA (New York, N.Y.)
|July 4, 2012
Summary
Box C/D small ribonucleoproteins (sRNPs) assemble as dimers, not monomers, when their guide RNAs contain internal loops. This dimeric structure is conserved across diverse archaeal species, clarifying sRNP architecture.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Box C/D small ribonucleoproteins (sRNPs) are crucial for RNA-guided 2'-O-ribose methylation in archaea and eukaryotes.
- Recent studies present conflicting models regarding box C/D sRNP assembly, with some suggesting monomeric and others dimeric structures.
Purpose of the Study:
- To investigate the role of the sRNA loop in determining box C/D sRNP assembly architecture.
- To resolve the controversy surrounding monomeric versus dimeric sRNP assembly.
Main Methods:
- sRNA mutagenesis
- Native gel electrophoresis
- Single-particle electron microscopy (EM)
- Reconstitution of box C/D sRNPs
Main Results:
- Box C/D sRNPs reconstituted with sRNAs possessing internal loops exclusively adopt a dimeric architecture (di-sRNP).
- This finding was consistent across three distinct archaeal species: Sulfolobus solfataricus, Pyrococcus abyssi, and Archaeoglobus fulgidus.
- The presence of an internal loop in the sRNA is identified as a key determinant for di-sRNP formation.
Conclusions:
- The dimeric architecture of box C/D sRNPs is broadly conserved across the archaeal domain.
- Internal loops within the guide sRNA are essential for promoting the formation of the dimeric sRNP structure.
- This study clarifies the functional assembly of box C/D sRNPs, resolving prior structural controversies.
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