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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
43
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pubmed:dateCreated |
2007-10-25
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pubmed:abstractText |
The eukaryotic core exosome (CE) is a conserved nine-subunit protein complex important for 3' end trimming and degradation of RNA. In yeast, the Rrp44 protein constitutively associates with the CE and provides the sole source of processive 3'-to-5' exoribonuclease activity. Here we present EM reconstructions of the core and Rrp44-bound exosome complexes. The two-lobed Rrp44 protein binds to the RNase PH domain side of the exosome and buttresses the bottom of the exosome-processing chamber. The Rrp44 C-terminal body part containing an RNase II-type active site is anchored to the exosome through a conserved set of interactions mainly to the Rrp45 and Rrp43 subunit, whereas the Rrp44 N-terminal head part is anchored to the Rrp41 subunit and may function as a roadblock to restrict access of RNA to the active site in the body region. The Rrp44-exosome (RE) architecture suggests an active site sequestration mechanism for strict control of 3' exoribonuclease activity in the RE complex.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-10222274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-10690410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-11027292,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-11809881,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-11922671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-12101094,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-14690599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-14749774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-15175755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-15231747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-15703439,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-16957732,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-17380186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-17643380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-3302267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-8160308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-9390555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-9562621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17942686-9582370
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16844-9
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pubmed:dateRevised |
2010-9-15
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pubmed:meshHeading |
pubmed-meshheading:17942686-Amino Acid Sequence,
pubmed-meshheading:17942686-Binding Sites,
pubmed-meshheading:17942686-Conserved Sequence,
pubmed-meshheading:17942686-Exoribonucleases,
pubmed-meshheading:17942686-Humans,
pubmed-meshheading:17942686-Models, Biological,
pubmed-meshheading:17942686-Models, Molecular,
pubmed-meshheading:17942686-Molecular Sequence Data,
pubmed-meshheading:17942686-Protein Binding,
pubmed-meshheading:17942686-Protein Conformation,
pubmed-meshheading:17942686-RNA, Fungal,
pubmed-meshheading:17942686-RNA Processing, Post-Transcriptional,
pubmed-meshheading:17942686-RNA Transport,
pubmed-meshheading:17942686-Saccharomyces cerevisiae,
pubmed-meshheading:17942686-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:17942686-Sequence Alignment,
pubmed-meshheading:17942686-Substrate Specificity
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pubmed:year |
2007
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pubmed:articleTitle |
Architecture of the yeast Rrp44 exosome complex suggests routes of RNA recruitment for 3' end processing.
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pubmed:affiliation |
Life Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA. hwwang@lbl.gov
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pubmed:publicationType |
Journal Article
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