Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-2-1
pubmed:abstractText
The 17 putative RNA helicases required for pre-rRNA processing are predicted to play a crucial role in ribosome biogenesis by driving structural rearrangements within preribosomes. To better understand the function of these proteins, we have generated a battery of mutations in five putative RNA helicases involved in 18S rRNA synthesis and analyzed their effects on cell growth and pre-rRNA processing. Our results define functionally important residues within conserved motifs and demonstrate that lethal mutations in predicted ATP binding-hydrolysis motifs often confer a dominant negative phenotype in vivo when overexpressed in a wild-type background. We show that dominant negative mutants delay processing of the 35S pre-rRNA and cause accumulation of pre-rRNA species that normally have low steady-state levels. Our combined results establish that not all conserved domains function identically in each protein, suggesting that the RNA helicases may have distinct biochemical properties and diverse roles in ribosome biogenesis.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10322435, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10373593, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10409734, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10504710, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10943890, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-10982841, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11101530, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11141562, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11156602, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11175897, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11222764, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11283007, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11545728, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11805826, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11839499, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11856747, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11861548, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11864606, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-11886864, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12067653, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12068309, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12150911, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12535527, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12742169, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-12957375, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-1378397, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-1385854, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-14759368, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-1502180, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-15049817, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-15120992, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-15201868, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-15523097, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-16449635, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-2046664, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-2442619, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-2846277, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-8112301, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-8413273, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-8419331, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-8774901, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-8910403, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9154839, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9199348, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9234672, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9315638, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9372960, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9524130, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9611193, http://linkedlifedata.com/resource/pubmed/commentcorrection/16449634-9717241
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1183-94
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis.
pubmed:affiliation
Molecular Biophysics & Biochemistry Department, Yale University School of Medicine, 333 Cedar St., SHM C-114, New Haven, CT 06520-8024, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't
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