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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2010-11-24
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pubmed:abstractText |
Archaeal and eukaryotic box C/D RNPs catalyze the 2'-O-methylation of ribosomal RNA, a modification that is essential for the correct folding and function of the ribosome. Each archaeal RNP contains three core proteins--L7Ae, Nop5, and fibrillarin (methyltransferase)--and a box C/D sRNA. Base-pairing between the sRNA guide region and the rRNA directs target site selection with the C/D and related C'/D' motifs functioning as protein binding sites. Recent structural analysis of in vitro assembled archaeal complexes has produced two divergent models of box C/D sRNP structure. In one model, the complex is proposed to be monomeric, while the other suggests a dimeric sRNP. The position of the RNA in the RNP is significantly different in each model. We have used UV-cross-linking to characterize protein-RNA contacts in the in vitro assembled Pyrococcus furiosus box C/D sRNP. The P. furiosus sRNP components assemble into complexes that are the expected size of di-sRNPs. Analysis of UV-induced protein-RNA cross-links revealed a novel interaction between the ALFR motif, in the Nop domain of Nop5, and the guide/spacer regions of the sRNA. We show that the ALFR motif and the spacer sequence adjacent to box C or C' are important for box C/D sRNP assembly in vitro. These data therefore reveal new RNA-protein contacts in the box C/D sRNP and suggest a role for Nop5 in substrate binding and/or release.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-10545122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-11006293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-11081632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-11842104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-11959980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12054894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12114023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12374753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12403468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12417735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12560482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12598892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-12881427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-15858219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-16256421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-16314460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-16601205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-16782898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-16857676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-17284456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-17412961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-17617422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-19111659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-19666563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-19745151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-8601279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-9843512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20962039-9848653
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Archaeal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Guide,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nucleolar,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/fibrillarin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1469-9001
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2341-8
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pubmed:dateRevised |
2011-7-28
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pubmed:meshHeading |
pubmed-meshheading:20962039-Base Sequence,
pubmed-meshheading:20962039-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:20962039-Cross-Linking Reagents,
pubmed-meshheading:20962039-Dimerization,
pubmed-meshheading:20962039-Efficiency,
pubmed-meshheading:20962039-Models, Biological,
pubmed-meshheading:20962039-Models, Molecular,
pubmed-meshheading:20962039-Molecular Sequence Data,
pubmed-meshheading:20962039-Nucleic Acid Conformation,
pubmed-meshheading:20962039-Protein Binding,
pubmed-meshheading:20962039-Pyrococcus furiosus,
pubmed-meshheading:20962039-RNA, Archaeal,
pubmed-meshheading:20962039-RNA, Guide,
pubmed-meshheading:20962039-RNA, Small Nucleolar,
pubmed-meshheading:20962039-Ribonucleoproteins, Small Nuclear
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pubmed:year |
2010
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pubmed:articleTitle |
A novel Nop5-sRNA interaction that is required for efficient archaeal box C/D sRNP formation.
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pubmed:affiliation |
Abteilung Zelluläre Biochemie, Max-Planck-Institute for Biophysical Chemistry, D-37077 Goettingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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