Source:http://linkedlifedata.com/resource/pubmed/id/17392269
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rdf:type | |
lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0033684,
umls-concept:C0035553,
umls-concept:C0205224,
umls-concept:C0450240,
umls-concept:C1145667,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1519613,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1706210,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2347567
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pubmed:issue |
20
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pubmed:dateCreated |
2007-5-14
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pubmed:abstractText |
The Drosophila gene, pixie, is an essential gene required for normal growth and translation. Pixie is the fly ortholog of human RLI, which was first identified as an RNase L inhibitor, and yeast Rli1p, which has recently been shown to play a role in translation initiation and ribosome biogenesis. These proteins are all soluble ATP-binding cassette proteins with two N-terminal iron-sulfur clusters. Here we demonstrate that Pixie can be isolated from cells in complex with eukaryotic translation initiation factor 3 and ribosomal proteins of the small subunit. In addition, our analysis of polysome profiles reveals that double-stranded RNA interference-mediated depletion of Pixie results in an increase in empty 80 S ribosomes and a corresponding decrease in polysomes. Thus Pixie is required for normal levels of translation initiation. We also find that Pixie associates with the 40 S subunit on sucrose density gradients in an ATP-dependent manner. Our observations are consistent with Pixie playing a catalytic role in the assembly of complexes required for translation initiation. Thus, the function of this soluble ATP-binding cassette domain protein family in translation initiation has been conserved from yeast through to higher eukaryotes.
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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/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-3,
http://linkedlifedata.com/resource/pubmed/chemical/pixie protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14752-60
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pubmed:meshHeading |
pubmed-meshheading:17392269-ATP-Binding Cassette Transporters,
pubmed-meshheading:17392269-Adenosine Triphosphate,
pubmed-meshheading:17392269-Animals,
pubmed-meshheading:17392269-Cell Line,
pubmed-meshheading:17392269-Drosophila Proteins,
pubmed-meshheading:17392269-Drosophila melanogaster,
pubmed-meshheading:17392269-Eukaryotic Initiation Factor-3,
pubmed-meshheading:17392269-Humans,
pubmed-meshheading:17392269-Peptide Chain Initiation, Translational,
pubmed-meshheading:17392269-Polyribosomes,
pubmed-meshheading:17392269-Protein Binding
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pubmed:year |
2007
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pubmed:articleTitle |
The essential Drosophila ATP-binding cassette domain protein, pixie, binds the 40 S ribosome in an ATP-dependent manner and is required for translation initiation.
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pubmed:affiliation |
Growth Regulation Laboratory, Cancer Research UK London Research Institute, P O Box 123, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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