A common core RNP structure shared between the small nucleoar box C/D RNPs and the spliceosomal U4 snRNP

被引:287
作者
Watkins, NJ
Ségault, V
Charpentier, B
Nottrott, S
Fabrizio, P
Bachi, A
Wilm, M
Rosbash, M
Branlant, C
Lührmann, R
机构
[1] Max Planck Inst Biophys Chem, Abt Zellulare Biochem, D-37070 Gottingen, Germany
[2] UHP Nancy 1, CNRS,Fac Sci, UMR 7567, Lab Maturat ARN & Enzymol Mol, F-54506 Vandoeuvre Les Nancy, France
[3] Brandeis Univ, Howard Hughes Med Inst, Dept Biol, Waltham, MA 02454 USA
[4] European Mol Biol Lab, D-69117 Heidelberg, Germany
关键词
D O I
10.1016/S0092-8674(00)00137-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (15.5kD 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 15.5kD binding site in the U4 snRNA. Consistent with this, the box C/D motif binds Snu13p/15.5kD 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.
引用
收藏
页码:457 / 466
页数:10
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