rdf:type |
|
lifeskim:mentions |
umls-concept:C0013879,
umls-concept:C0015576,
umls-concept:C0035668,
umls-concept:C0085762,
umls-concept:C0149561,
umls-concept:C0162807,
umls-concept:C0179400,
umls-concept:C0205224,
umls-concept:C0751969,
umls-concept:C1519249,
umls-concept:C1704788
|
pubmed:issue |
7
|
pubmed:dateCreated |
1997-5-5
|
pubmed:databankReference |
|
pubmed:abstractText |
Eukaryotic cells contain a large number of small nucleolar RNAs (snoRNAs). A major family of snoRNAs features a consensus ACA motif positioned 3 nucleotides from the 3' end of the RNA. In this study we have characterized nine novel human ACA snoRNAs (U64-U72). Structural probing of U64 RNA followed by systematic computer modeling of all known box ACA snoRNAs revealed that this class of snoRNAs is defined by a phylogenetically conserved secondary structure. The ACA snoRNAs fold into two hairpin structures connected by a single-stranded hinge region and followed by a short 3' tail. The hinge region carries an evolutionarily conserved sequence motif, called box H (consensus, AnAnnA). The H box, probably in concert with the flanking helix structures and the ACA box characterized previously, plays an essential role in the accumulation of human U64 intronic snoRNA. The correct processing of a yeast ACA snoRNA, snR36, in mammalian cells demonstrated that the cis- and trans-acting elements required for processing and accumulation of ACA snoRNAs are evolutionarily conserved. The notion that ACA snoRNAs share a common secondary structure and conserved box elements that likely function as binding sites for common proteins (e.g., GAR1) suggests that these RNAs possess closely related nucleolar functions.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAR1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nucleolar,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/fibrillarin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0890-9369
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
11
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
941-56
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:9106664-Base Sequence,
pubmed-meshheading:9106664-Biological Evolution,
pubmed-meshheading:9106664-Cell Nucleolus,
pubmed-meshheading:9106664-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:9106664-Computer Simulation,
pubmed-meshheading:9106664-Conserved Sequence,
pubmed-meshheading:9106664-Fungal Proteins,
pubmed-meshheading:9106664-HeLa Cells,
pubmed-meshheading:9106664-Humans,
pubmed-meshheading:9106664-Introns,
pubmed-meshheading:9106664-Models, Genetic,
pubmed-meshheading:9106664-Models, Molecular,
pubmed-meshheading:9106664-Molecular Sequence Data,
pubmed-meshheading:9106664-Multigene Family,
pubmed-meshheading:9106664-Nuclear Proteins,
pubmed-meshheading:9106664-Nucleic Acid Conformation,
pubmed-meshheading:9106664-Protein Binding,
pubmed-meshheading:9106664-RNA, Small Nuclear,
pubmed-meshheading:9106664-RNA Processing, Post-Transcriptional,
pubmed-meshheading:9106664-Ribonucleoproteins, Small Nucleolar,
pubmed-meshheading:9106664-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9106664-Species Specificity
|
pubmed:year |
1997
|
pubmed:articleTitle |
The family of box ACA small nucleolar RNAs is defined by an evolutionarily conserved secondary structure and ubiquitous sequence elements essential for RNA accumulation.
|
pubmed:affiliation |
Laboratoire de Biologie Moléculaire Eucaryote du Centre National de laRecherche (CNRS), Université Paul Sabatier, Toulouse, France.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|