The box C/D snoRNAs function in directing 2'-O-methylation and/or as chaperones in the processing of ribosomal RNA. We show here that Snu13p (15.5 kD in human), a component of the U4/U6.U5 tri-snRNP, is also associated with the box C/D snoRNAs. Indeed, genetic depletion of Snu13p in yeast leads to a major defect in RNA metabolism. The box C/D motif can be folded into a stem-internal loop-stem structure, almost identical to the 15.5 kD binding site in the U4 snRNA. Consistent with this, the box C/D motif binds Snu13p/ 15.5 kD in vitro. The similarities in structure and function observed between the U4 snRNP (chaperone for U6) and the box C/D snoRNPs raises the interesting possibility that these particles may have evolved from a common ancestral RNP.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
The box C/D snoRNAs function in directing 2'-O-methylation and/or as chaperones in the processing of ribosomal RNA. We show here that Snu13p (15.5 kD in human), a component of the U4/U6.U5 tri-snRNP, is also associated with the box C/D snoRNAs. Indeed, genetic depletion of Snu13p in yeast leads to a major defect in RNA metabolism. The box C/D motif can be folded into a stem-internal loop-stem structure, almost identical to the 15.5 kD binding site in the U4 snRNA. Consistent with this, the box C/D motif binds Snu13p/ 15.5 kD in vitro. The similarities in structure and function observed between the U4 snRNP (chaperone for U6) and the box C/D snoRNPs raises the interesting possibility that these particles may have evolved from a common ancestral RNP.
|
| skos:exactMatch | |
| uniprot:name |
Cell
|
| uniprot:author |
Bachi A.,
Branlant C.,
Charpentier B.,
Fabrizio P.,
Luehrmann R.,
Nottrott S.,
Rosbash M.,
Segault V.,
Watkins N.J.,
Wilm M.
|
| uniprot:date |
2000
|
| uniprot:pages |
457-466
|
| uniprot:title |
A common core RNP structure shared between the small nucleoar box C/D RNPs and the spliceosomal U4 snRNP.
|
| uniprot:volume |
103
|
| dc-term:identifier |
doi:10.1016/S0092-8674(00)00137-9
|