Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit.
Identifieur interne : 002954 ( Main/Curation ); précédent : 002953; suivant : 002955Ribosome performance is enhanced by a rich cluster of pseudouridines in the A-site finger region of the large subunit.
Auteurs : Dorota Piekna-Przybylska [États-Unis] ; Piotr Przybylski ; Agnès Baudin-Baillieu ; Jean-Pierre Rousset ; Maurille J. FournierSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- ARN fongique (), Conformation d'acide nucléique, Conformation moléculaire, Données de séquences moléculaires, Modèles génétiques, Modèles moléculaires, Petit ARN nucléolaire (), Plasmides (métabolisme), Polyribosomes (), Pseudouridine (), Ribosomes (), Saccharomyces cerevisiae (métabolisme), Structure tertiaire des protéines, Séquence nucléotidique, Température.
- MESH :
- métabolisme : Plasmides, Saccharomyces cerevisiae.
- ARN fongique, Conformation d'acide nucléique, Conformation moléculaire, Données de séquences moléculaires, Modèles génétiques, Modèles moléculaires, Petit ARN nucléolaire, Polyribosomes, Pseudouridine, Ribosomes, Structure tertiaire des protéines, Séquence nucléotidique, Température.
English descriptors
- KwdEn :
- Base Sequence, Models, Genetic, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Nucleic Acid Conformation, Plasmids (metabolism), Polyribosomes (chemistry), Protein Structure, Tertiary, Pseudouridine (chemistry), RNA, Fungal (chemistry), RNA, Small Nucleolar (chemistry), Ribosomes (chemistry), Saccharomyces cerevisiae (metabolism), Temperature.
- MESH :
- chemical , chemistry : Pseudouridine, RNA, Fungal, RNA, Small Nucleolar.
- chemistry : Polyribosomes, Ribosomes.
- metabolism : Plasmids, Saccharomyces cerevisiae.
- Base Sequence, Models, Genetic, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Nucleic Acid Conformation, Protein Structure, Tertiary, Temperature.
Abstract
The large subunit rRNA in eukaryotes contains an unusually dense cluster of 8-10 pseudouridine (Psi) modifications located in a three-helix structure (H37-H39) implicated in several functions. This region is dominated by a long flexible helix (H38) known as the "A-site finger" (ASF). The ASF protrudes from the large subunit just above the A-site of tRNA binding, interacts with 5 S rRNA and tRNA, and through the terminal loop, forms a bridge (B1a) with the small subunit. In yeast, the three-helix domain contains 10 Psis and 6 are concentrated in the ASF helix (3 of the ASF Psis are conserved among eukaryotes). Here, we show by genetic depletion analysis that the Psis in the ASF helix and adjoining helices are not crucial for cell viability; however, their presence notably enhances ribosome fitness. Depleting different combinations of Psis suggest that the modification pattern is important and revealed that loss of multiple Psis negatively influences ribosome performance. The effects observed include slower cell growth (reduced rates up to 23% at 30 degrees C and 40-50% at 37 degrees C and 11 degrees C), reduced level of the large subunit (up to 17%), impaired polysome formation (appearance of half-mers), reduced translation activity (up to 20% at 30 degrees C and 25% at 11 degrees C), and increased sensitivity to ribosome-based drugs. The results indicate that the Psis in the three-helix region improve fitness of a eukaryotic ribosome.
DOI: 10.1074/jbc.M803049200
PubMed: 18611858
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pubmed:18611858Le document en format XML
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<term>Molecular Sequence Data</term>
<term>Nucleic Acid Conformation</term>
<term>Plasmids (metabolism)</term>
<term>Polyribosomes (chemistry)</term>
<term>Protein Structure, Tertiary</term>
<term>Pseudouridine (chemistry)</term>
<term>RNA, Fungal (chemistry)</term>
<term>RNA, Small Nucleolar (chemistry)</term>
<term>Ribosomes (chemistry)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Temperature</term>
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<term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Modèles génétiques</term>
<term>Modèles moléculaires</term>
<term>Petit ARN nucléolaire ()</term>
<term>Plasmides (métabolisme)</term>
<term>Polyribosomes ()</term>
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<term>Séquence nucléotidique</term>
<term>Température</term>
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<term>Saccharomyces cerevisiae</term>
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<term>Saccharomyces cerevisiae</term>
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<term>Models, Genetic</term>
<term>Models, Molecular</term>
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<term>Molecular Sequence Data</term>
<term>Nucleic Acid Conformation</term>
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<term>Modèles génétiques</term>
<term>Modèles moléculaires</term>
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<term>Polyribosomes</term>
<term>Pseudouridine</term>
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<front><div type="abstract" xml:lang="en">The large subunit rRNA in eukaryotes contains an unusually dense cluster of 8-10 pseudouridine (Psi) modifications located in a three-helix structure (H37-H39) implicated in several functions. This region is dominated by a long flexible helix (H38) known as the "A-site finger" (ASF). The ASF protrudes from the large subunit just above the A-site of tRNA binding, interacts with 5 S rRNA and tRNA, and through the terminal loop, forms a bridge (B1a) with the small subunit. In yeast, the three-helix domain contains 10 Psis and 6 are concentrated in the ASF helix (3 of the ASF Psis are conserved among eukaryotes). Here, we show by genetic depletion analysis that the Psis in the ASF helix and adjoining helices are not crucial for cell viability; however, their presence notably enhances ribosome fitness. Depleting different combinations of Psis suggest that the modification pattern is important and revealed that loss of multiple Psis negatively influences ribosome performance. The effects observed include slower cell growth (reduced rates up to 23% at 30 degrees C and 40-50% at 37 degrees C and 11 degrees C), reduced level of the large subunit (up to 17%), impaired polysome formation (appearance of half-mers), reduced translation activity (up to 20% at 30 degrees C and 25% at 11 degrees C), and increased sensitivity to ribosome-based drugs. The results indicate that the Psis in the three-helix region improve fitness of a eukaryotic ribosome.</div>
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