The multistructural forms of box C/D ribonucleoprotein particles.

Publication Type:

Journal Article


RNA, Volume 24, Issue 12, p.1625-1633 (2018)


Archaea, Nuclear Proteins, Nucleic Acid Conformation, Ribonucleoproteins, Ribonucleoproteins, Small Nucleolar, Ribosomes, RNA, Archaeal, RNA, Ribosomal, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins


<p>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.</p>