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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6048
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pubmed:dateCreated |
2011-9-9
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pubmed:abstractText |
Ribosome assembly in eukaryotes requires approximately 200 essential assembly factors (AFs) and occurs through ordered events that initiate in the nucleolus and culminate in the cytoplasm. Here, we present the electron cryo-microscopy (cryo-EM) structure of a late cytoplasmic 40S ribosome assembly intermediate from Saccharomyces cerevisiae at 18 angstrom resolution. We obtained cryo-EM reconstructions of preribosomal complexes lacking individual components to define the positions of all seven AFs bound to this intermediate. These late-binding AFs are positioned to prevent each step in the translation initiation pathway. Together, they obstruct the binding sites for initiation factors, prevent the opening of the messenger RNA channel, block 60S subunit joining, and disrupt the decoding site. These redundant mechanisms probably ensure that pre-40S particles do not enter the translation pathway, which would result in their rapid degradation.
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pubmed:grant |
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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/DIM1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-1,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-3,
http://linkedlifedata.com/resource/pubmed/chemical/LTV1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/NOB1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rio2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eukaryotic peptide initiation...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
9
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pubmed:volume |
333
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1449-53
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pubmed:meshHeading |
pubmed-meshheading:21835981-Binding Sites,
pubmed-meshheading:21835981-Cryoelectron Microscopy,
pubmed-meshheading:21835981-Eukaryotic Initiation Factor-1,
pubmed-meshheading:21835981-Eukaryotic Initiation Factor-3,
pubmed-meshheading:21835981-Image Processing, Computer-Assisted,
pubmed-meshheading:21835981-Methyltransferases,
pubmed-meshheading:21835981-Models, Molecular,
pubmed-meshheading:21835981-Nuclear Proteins,
pubmed-meshheading:21835981-Peptide Chain Initiation, Translational,
pubmed-meshheading:21835981-Protein-Serine-Threonine Kinases,
pubmed-meshheading:21835981-RNA, Fungal,
pubmed-meshheading:21835981-RNA, Messenger,
pubmed-meshheading:21835981-Ribosomal Proteins,
pubmed-meshheading:21835981-Ribosome Subunits, Small, Eukaryotic,
pubmed-meshheading:21835981-Saccharomyces cerevisiae,
pubmed-meshheading:21835981-Saccharomyces cerevisiae Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates.
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pubmed:affiliation |
Chemical Biology Doctoral Program, University of Michigan, Ann Arbor, MI 48109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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