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Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.

Identifieur interne : 000041 ( Hal/Curation ); précédent : 000040; suivant : 000042

Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.

Auteurs : Jean-Paul Armache [Allemagne] ; Alexander Jarasch [Allemagne] ; Andreas M. Anger [Allemagne] ; Elizabeth Villa [Allemagne] ; Thomas Becker [Allemagne] ; Shashi Bhushan [Allemagne] ; Fabrice Jossinet [France] ; Michael Habeck [France] ; Gülcin Dindar [Allemagne] ; Sibylle Franckenberg [Allemagne] ; Viter Marquez [Allemagne] ; Thorsten Mielke [Allemagne] ; Michael Thomm [Allemagne] ; Otto Berninghausen [Allemagne] ; Birgitta Beatrix [Allemagne] ; Johannes Söding [Allemagne] ; Eric Westhof [France] ; Daniel N. Wilson [Allemagne] ; Roland Beckmann [Allemagne]

Source :

RBID : Hal:hal-00530586

Abstract

Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98% of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES-ES and r-protein-ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.


Url:
DOI: 10.1073/pnas.1009999107

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Hal:hal-00530586

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<name sortKey="Beckmann, Roland" sort="Beckmann, Roland" uniqKey="Beckmann R" first="Roland" last="Beckmann">Roland Beckmann</name>
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<idno type="DOI">10.1073/pnas.1009999107</idno>
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<title level="j">Proceedings of the National Academy of Sciences of the United States of America </title>
<idno type="ISSN">0027-8424</idno>
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<date type="datePub">2010-10-27</date>
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<p>Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98% of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES-ES and r-protein-ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.</p>
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<title xml:lang="en">Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.</title>
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<forename type="first">Jean-Paul</forename>
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<forename type="first">Alexander</forename>
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<forename type="first">Andreas M</forename>
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<forename type="first">Elizabeth</forename>
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<forename type="first">Thomas</forename>
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<forename type="first">Shashi</forename>
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<forename type="first">Otto</forename>
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<forename type="first">Birgitta</forename>
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<forename type="first">Johannes</forename>
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<forename type="first">Eric</forename>
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<forename>Danièle</forename>
<surname>Werling</surname>
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<date type="whenReleased">2010-10-29 13:50:59</date>
<date type="whenProduced">2010-10-27</date>
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<idno type="halRefHtml">Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2010, epub ahead of print. ⟨10.1073/pnas.1009999107⟩</idno>
<idno type="halRef">Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2010, epub ahead of print. ⟨10.1073/pnas.1009999107⟩</idno>
</publicationStmt>
<seriesStmt>
<idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
<idno type="stamp" n="PASTEUR">Institut Pasteur</idno>
<idno type="stamp" n="RIIP_PARIS">Institut Pasteur de Paris</idno>
<idno type="stamp" n="UNIV-STRASBG">Université de Strasbourg</idno>
<idno type="stamp" n="SITE-ALSACE">Archive ouverte du site Alsace</idno>
</seriesStmt>
<notesStmt>
<note type="audience" n="2">International</note>
<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
</notesStmt>
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<analytic>
<title xml:lang="en">Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.</title>
<author role="aut">
<persName>
<forename type="first">Jean-Paul</forename>
<surname>Armache</surname>
</persName>
<idno type="halauthorid">482490</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Alexander</forename>
<surname>Jarasch</surname>
</persName>
<idno type="halauthorid">482489</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Andreas M</forename>
<surname>Anger</surname>
</persName>
<idno type="halauthorid">538127</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Elizabeth</forename>
<surname>Villa</surname>
</persName>
<idno type="halauthorid">538128</idno>
<affiliation ref="#struct-130144"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Thomas</forename>
<forename type="middle">S.</forename>
<surname>Becker</surname>
</persName>
<idno type="halauthorid">202671</idno>
<affiliation ref="#struct-460216"></affiliation>
<affiliation ref="#struct-51800"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Shashi</forename>
<surname>Bhushan</surname>
</persName>
<idno type="halauthorid">482488</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Fabrice</forename>
<surname>Jossinet</surname>
</persName>
<idno type="halauthorid">202811</idno>
<affiliation ref="#struct-93780"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Michael</forename>
<surname>Habeck</surname>
</persName>
<idno type="halauthorid">350241</idno>
<affiliation ref="#struct-15014"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Gülcin</forename>
<surname>Dindar</surname>
</persName>
<idno type="halauthorid">538129</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Sibylle</forename>
<surname>Franckenberg</surname>
</persName>
<idno type="halauthorid">538130</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Viter</forename>
<surname>Marquez</surname>
</persName>
<idno type="halauthorid">538131</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Thorsten</forename>
<surname>Mielke</surname>
</persName>
<idno type="halauthorid">152230</idno>
<affiliation ref="#struct-333449"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Michael</forename>
<surname>Thomm</surname>
</persName>
<idno type="halauthorid">538132</idno>
<affiliation ref="#struct-131269"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Otto</forename>
<surname>Berninghausen</surname>
</persName>
<idno type="halauthorid">482492</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Birgitta</forename>
<surname>Beatrix</surname>
</persName>
<idno type="halauthorid">538133</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Johannes</forename>
<surname>Söding</surname>
</persName>
<idno type="halauthorid">538134</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Eric</forename>
<surname>Westhof</surname>
</persName>
<idno type="halauthorid">122890</idno>
<affiliation ref="#struct-93780"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Daniel N</forename>
<surname>Wilson</surname>
</persName>
<idno type="halauthorid">538135</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
<author role="aut">
<persName>
<forename type="first">Roland</forename>
<surname>Beckmann</surname>
</persName>
<idno type="halauthorid">482496</idno>
<affiliation ref="#struct-460216"></affiliation>
</author>
</analytic>
<monogr>
<idno type="halJournalId" status="VALID">7969</idno>
<idno type="issn">0027-8424</idno>
<idno type="eissn">1091-6490</idno>
<title level="j">Proceedings of the National Academy of Sciences of the United States of America </title>
<imprint>
<publisher>National Academy of Sciences</publisher>
<biblScope unit="pp">epub ahead of print</biblScope>
<date type="datePub">2010-10-27</date>
<date type="dateEpub">2010-10-27</date>
</imprint>
</monogr>
<idno type="doi">10.1073/pnas.1009999107</idno>
<idno type="pubmed">20980660</idno>
</biblStruct>
</sourceDesc>
<profileDesc>
<langUsage>
<language ident="en">English</language>
</langUsage>
<textClass>
<classCode scheme="halDomain" n="sdv.bbm">Life Sciences [q-bio]/Biochemistry, Molecular Biology</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en">
<p>Protein biosynthesis, the translation of the genetic code into polypeptides, occurs on ribonucleoprotein particles called ribosomes. Although X-ray structures of bacterial ribosomes are available, high-resolution structures of eukaryotic 80S ribosomes are lacking. Using cryoelectron microscopy and single-particle reconstruction, we have determined the structure of a translating plant (Triticum aestivum) 80S ribosome at 5.5-Å resolution. This map, together with a 6.1-Å map of a Saccharomyces cerevisiae 80S ribosome, has enabled us to model ∼98% of the rRNA. Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES-ES and r-protein-ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.</p>
</abstract>
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</hal>
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