Source:http://linkedlifedata.com/resource/pubmed/id/16095611
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-8-30
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pubmed:abstractText |
Previous work suggested that the release of the nucleolar Tif6 from nascent 60 S subunits occurs in the cytoplasm and requires the cytoplasmic EF-2-like GTPase, Efl1. To check whether this release involves an rRNA structural rearrangement mediated by Efl1, we analyzed the rRNA conformation of the GTPase center of 80 S ribosomes in three contexts: wild-type, Deltaefl1 and a dominant suppressor R1 of Deltaefl1. This analysis was restricted to domain II and VI of 25 S rRNA. The rRNA analysis of R1 ribosomes allows us to distinguish the effects due to depletion of Efl1 from the resulting nucleolar deficit of Tif6. Efl1 inhibits the EF-2 GTPase activity, suggesting that the two proteins share a similar ribosome-binding site. The 80 S ribosomes from either type failed to show any difference of conformation in the two rRNA domains analyzed. However, the same analysis performed on the pool of free 60 S subunits reveals several rRNA conformational differences between wild-type and Deltaefl1 subunits, whereas that from the suppressor strain is similar to wild-type. This suggests that the nucleolar deficit of Tif6 during assembly of the 60 S preribosomes is responsible for the changes in rRNA conformation observed in Deltaefl1 60 S subunits. We also purified 60 S preribosomes from the three genetic contexts by TAP-tagging Tif6. The protein content of 60 S preribosomes associated with Tif6p in a Deltaefl1 strain are obtained at a lower yield but have, surprisingly, a protein composition that is a priori similar to that of wild-type and the suppressor strain.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Intermediate Filament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TIF6 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
352
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
355-69
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16095611-Binding Sites,
pubmed-meshheading:16095611-Carrier Proteins,
pubmed-meshheading:16095611-GTP Phosphohydrolases,
pubmed-meshheading:16095611-Intermediate Filament Proteins,
pubmed-meshheading:16095611-Mutation,
pubmed-meshheading:16095611-Nucleic Acid Conformation,
pubmed-meshheading:16095611-Phosphoproteins,
pubmed-meshheading:16095611-RNA, Fungal,
pubmed-meshheading:16095611-RNA, Ribosomal,
pubmed-meshheading:16095611-Ribosomal Proteins,
pubmed-meshheading:16095611-Ribosomes,
pubmed-meshheading:16095611-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16095611-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2005
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pubmed:articleTitle |
Deletion of EFL1 results in heterogeneity of the 60 S GTPase-associated rRNA conformation.
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pubmed:affiliation |
UPR no. 9002 du CNRS, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes, 67084 Strasbourg Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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