The multistructural forms of box C/D ribonucleoprotein particles
- 1Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306, USA
- 2Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA
- Corresponding author: hong.li{at}fsu.edu
Abstract
Structural biology studies of archaeal and yeast box C/D ribonucleoprotein particles (RNPs) reveal a surprisingly wide range of forms. If form ever follows function, the different structures of box C/D small ribonucleoprotein particles (snoRNPs) may reflect their versatile functional roles beyond what has been recognized. A large majority of box C/D RNPs serve to site-specifically methylate the ribosomal RNA, typically as independent complexes. Select members of the box C/D snoRNPs also are essential components of the megadalton RNP enzyme, the small subunit processome that is responsible for processing ribosomal RNA. Other box C/D RNPs continue to be uncovered with either unexpected or unknown functions. We summarize currently known box C/D RNP structures in this review and identify the Nop56/58 and box C/D RNA subunits as the key elements underlying the observed structural diversity, and likely, the diverse functional roles of box C/D RNPs.
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Article is online at http://www.rnajournal.org/cgi/doi/10.1261/rna.068312.118.
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