An in vivo and in vitro structure-function analysis of the Saccharomyces cerevisiae U3A snoRNP: protein-RNA contacts and base-pair interaction with the pre-ribosomal RNA
Identifieur interne : 00BC75 ( Main/Exploration ); précédent : 00BC74; suivant : 00BC76An in vivo and in vitro structure-function analysis of the Saccharomyces cerevisiae U3A snoRNP: protein-RNA contacts and base-pair interaction with the pre-ribosomal RNA
Auteurs : Agnès Méreau [France] ; Régis Fournier [France] ; Anne Grégoire [France] ; Annie Mougin [France] ; Patrizia Fabrizio [Allemagne] ; Reinhard Lührmann [Allemagne] ; Christiane Branlant [France]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 1997.
English descriptors
- KwdEn :
- Teeft :
- Ares, Baserga, Beltrame, Beltrame tollervey, Biol, Brillarin, Cerevisiae, Cleavage, Cruciform, Cruciform structure, Deletion, Digestion, Embo, Enzymatic digestion, Ethanol, Functional importance, Functionality, Good agreement, Helical, Helix, Heterologous, Heterologous helices, Hughes ares, Hybridization, Internal loop, Mutation, Mutational analysis, Nucl, Nucleolar, Parker steitz, Phenol, Phenotype, Phylogenetically, Plasmid, Present results, Primer, Putative helix, Ribosomal, Rna, Rnase, Rnase cleavages, Rnase digestions, Rrna, Rrna sequences, Saccharomyces, Saccharomyces cerevisiae, Secondary structure, Segault, Small nucleolar, Snorna, Snorna gene, Snorna molecules, Snorna sequences, Snorna transcript, Snorna variants, Snornas, Snornp, Snornp particle, Snornp proteins, Snornps, Snrna, Sodium acetate, Steitz, Terminal region, Tollervey, U3snornp, Variant, Vertebrate, Vivo, Xenopus, Yeast.
Abstract
Abstract: The structure and accessibility of the S. cerevisiae U3A snoRNA was studied in semi-purified U3A snoRNPs using both chemical and enzymatic probes and in vivo using DMS as the probe. The results obtained show thatS. cerevisiae U3A snoRNA is composed of a short 5′ domain with two stem-loop structures containing the phylogenetically conserved boxes A′ and A and a large cruciform 3′ domain containing boxes B, C, C′ and D. A precise identification of RNA-protein contacts is provided. Protection by proteins in the snoRNP and in vivo are nearly identical and were exclusively found in the 3′ domain. There are two distinct protein anchoring sites: (i), box C′ and its surrounding region, this site probably includes box D, (ii) the boxes B and C pair and the bases of stem-loop 2 and 4. Box C′ is wrapped by the proteins. RNA-protein interactions are more loose at the level of boxes C and D and a box C and D interaction is preserved in the snoRNP. In accord with this location of the protein binding sites, an in vivo mutational analysis showed that box C′ is important for U3A snoRNA accumulation, whereas mutations in the 5′ domain have little effect on RNA stability. Our in vivo probing experiments strongly suggest that, in exponentially growing cells, most of the U3A snoRNA molecules are involved in the 10-bp interaction with the 5′-ETS region and in two of the interactions recently proposed with 18S rRNA sequences. Our experimental study leads to a slightly revised version of the model of interaction proposed by J. Hughes. Single-stranded segments linking the heterologous helices are highly sensitive to DMS in vivo and their functional importance was tested by a mutational analysis.
Url:
DOI: 10.1006/jmbi.1997.1320
Affiliations:
- Allemagne, France
- District de Giessen, Grand Est, Hesse (Land), Lorraine (région)
- Marbourg, Vandœuvre-lès-Nancy
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Le document en format XML
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<term>RNA secondary structure</term>
<term>S. cerevisiae</term>
<term>SnoRNA</term>
<term>U3 snoRNP</term>
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<term>Beltrame tollervey</term>
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<term>Brillarin</term>
<term>Cerevisiae</term>
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<term>Enzymatic digestion</term>
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<term>Mutation</term>
<term>Mutational analysis</term>
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<term>Present results</term>
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<term>Putative helix</term>
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<term>Rnase</term>
<term>Rnase cleavages</term>
<term>Rnase digestions</term>
<term>Rrna</term>
<term>Rrna sequences</term>
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<front><div type="abstract" xml:lang="en">Abstract: The structure and accessibility of the S. cerevisiae U3A snoRNA was studied in semi-purified U3A snoRNPs using both chemical and enzymatic probes and in vivo using DMS as the probe. The results obtained show thatS. cerevisiae U3A snoRNA is composed of a short 5′ domain with two stem-loop structures containing the phylogenetically conserved boxes A′ and A and a large cruciform 3′ domain containing boxes B, C, C′ and D. A precise identification of RNA-protein contacts is provided. Protection by proteins in the snoRNP and in vivo are nearly identical and were exclusively found in the 3′ domain. There are two distinct protein anchoring sites: (i), box C′ and its surrounding region, this site probably includes box D, (ii) the boxes B and C pair and the bases of stem-loop 2 and 4. Box C′ is wrapped by the proteins. RNA-protein interactions are more loose at the level of boxes C and D and a box C and D interaction is preserved in the snoRNP. In accord with this location of the protein binding sites, an in vivo mutational analysis showed that box C′ is important for U3A snoRNA accumulation, whereas mutations in the 5′ domain have little effect on RNA stability. Our in vivo probing experiments strongly suggest that, in exponentially growing cells, most of the U3A snoRNA molecules are involved in the 10-bp interaction with the 5′-ETS region and in two of the interactions recently proposed with 18S rRNA sequences. Our experimental study leads to a slightly revised version of the model of interaction proposed by J. Hughes. Single-stranded segments linking the heterologous helices are highly sensitive to DMS in vivo and their functional importance was tested by a mutational analysis.</div>
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