Source:http://linkedlifedata.com/resource/pubmed/id/15231838
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
36
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pubmed:dateCreated |
2004-8-30
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pubmed:abstractText |
Here we report the functional characterization of Pwp2, an evolutionary conserved component of the 90 S pre-ribosome. Conditional depletion of the Pwp2 protein in yeast specifically impairs pre-rRNA proccessing at sites A(0), A(1), and A(2), leading to a strong decrease in 18 S rRNA and 40 S ribosomal subunit levels. Pre-ribosomal particle sedimentation analysis indicated that these defects are caused by a block in the formation of 90 S pre-ribosomes. We demonstrate that in Pwp2-depleted cells the U3 small nucleolar ribonucleoprotein is not able to interact with the 35 S pre-rRNA and accumulates as a free complex. Similarly, other 90 S particle components such as Imp3 and Imp4 do not associate with the pre-rRNA precursor in the absence of Pwp2. In addition, we have found that after blocking U3 ribonucleoprotein assembly, Pwp2 predominantly accumulates as a complex in association with five proteins: Dip2, Utp6, Utp13, Utp18, and Utp21. Immunoprecipitation and gradient sedimentation analysis revealed that this Pwp2 small subcomplex is capable of interacting directly with the 35 S pre-rRNA 5' end. Taken together, these results indicate that Pwp2 forms part of a stable particle subunit independent of the U3 small nucleolar ribonucleoprotein that is essential for the initial assembly steps of the 90 S pre-ribosome.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PWP2 protein, S cerevisiae,
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
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37385-97
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15231838-Base Sequence,
pubmed-meshheading:15231838-DNA Primers,
pubmed-meshheading:15231838-Hydrolysis,
pubmed-meshheading:15231838-Nuclear Proteins,
pubmed-meshheading:15231838-RNA, Ribosomal,
pubmed-meshheading:15231838-Ribosomal Proteins,
pubmed-meshheading:15231838-Ribosomes,
pubmed-meshheading:15231838-Saccharomyces cerevisiae,
pubmed-meshheading:15231838-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15231838-Sequence Deletion
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pubmed:year |
2004
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pubmed:articleTitle |
Functional characterization of Pwp2, a WD family protein essential for the assembly of the 90 S pre-ribosomal particle.
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pubmed:affiliation |
Centro de Investigación del Cáncer and Instituto de Biología Molecular y Celular del Cáncer, University of Salamanca-CSIC, Campus Unamuno, E-37007 Salamanca, Spain. mdosil@usal.es
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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