| In vitro assembly of the mouse U14 snoRNP core complex and identification of a 65-kDa box C/D-binding protein. | |
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MedLine Citation:
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PMID: 9582099 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The eukaryotic nucleolus contains a diverse population of small nucleolar RNAs (snoRNAs) that have been categorized into two major families based on evolutionarily conserved sequence elements. U14 snoRNA is a member of the larger, box C/D snoRNA family and possesses nucleotide box C and D consensus sequences. In previous studies, we have defined a U14 box C/D core motif that is essential for intronic U14 snoRNA processing. These studies also revealed that nuclear proteins that recognize boxes C/D are required. We have now established an in vitro U14 snoRNP assembly system to characterize protein binding. Electrophoretic mobility-shift analysis demonstrated that all the sequences and structures of the box C/D core motif required for U14 processing are also necessary for protein binding and snoRNP assembly. These required elements include a base paired 5',3' terminal stem and the phylogenetically conserved nucleotides of boxes C and D. The ability of other box C/D snoRNAs to compete for protein binding demonstrated that the box C/D core motif-binding proteins are common to this family of snoRNAs. UV crosslinking of nuclear proteins bound to the U14 core motif identified a 65-kDa mouse snoRNP protein that requires boxes C and D for binding. Two additional core motif proteins of 55 and 50 kDa were also identified by biochemical fractionation of the in vitro-assembled U14 snoRNP complex. Thus, the U14 snoRNP core complex is a multiprotein particle whose assembly requires nucleotide boxes C and D. |
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Authors:
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N J Watkins; D R Newman; J F Kuhn; E S Maxwell |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: RNA (New York, N.Y.) Volume: 4 ISSN: 1355-8382 ISO Abbreviation: RNA Publication Date: 1998 May |
Date Detail:
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Created Date: 1998-05-27 Completed Date: 1998-05-27 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 9509184 Medline TA: RNA Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 582-93 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, North Carolina State University, Raleigh 27695-7622, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Ascitic Fluid / cytology Cell Extracts Cross-Linking Reagents Hela Cells Humans Mice Molecular Weight Nucleic Acid Conformation Oocytes Protein Binding RNA, Small Nuclear / chemistry, genetics, metabolism* RNA-Binding Proteins / chemistry, isolation & purification, metabolism* Ribonucleoproteins, Small Nuclear / biosynthesis*, chemistry Ultraviolet Rays Xenopus |
| Chemical | |
Reg. No./Substance:
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0/Cell Extracts; 0/Cross-Linking Reagents; 0/RNA, Small Nuclear; 0/RNA-Binding Proteins; 0/Ribonucleoproteins, Small Nuclear |
| Comments/Corrections | |
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