rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
4
|
pubmed:dateCreated |
2007-5-28
|
pubmed:abstractText |
RNA interference is a conserved pathway of sequence-specific gene silencing that depends on small guide RNAs and the action of proteins assembled in the RNA-induced silencing complex (RISC). Minimally, the action of RISC requires the endonucleolytic slicer activity of Argonaute2 (Ago2) directed to RNA targets whose sequences are complementary to RISC-incorporated small RNA. To identify RISC components in human cells, we developed an affinity-purification strategy to isolate siRNA-programmed RISC. Here we report the identification of RNA helicase A (RHA) as a human RISC-associated factor. We show that RHA interacts in human cells with siRNA, Ago2, TRBP, and Dicer and functions in the RNAi pathway. In RHA-depleted cells, RNAi was reduced as a consequence of decreased intracellular concentration of active RISC assembled with the guide-strand RNA and Ago2. Our results identify RHA as a RISC component and demonstrate that RHA functions in RISC as an siRNA-loading factor.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Argonaute Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DHX9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/EIF2C2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SCPEP1 protein, human
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1097-2765
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
26
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
523-37
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:17531811-Argonaute Proteins,
pubmed-meshheading:17531811-Carboxypeptidases,
pubmed-meshheading:17531811-Cell Line,
pubmed-meshheading:17531811-DEAD-box RNA Helicases,
pubmed-meshheading:17531811-Eukaryotic Initiation Factor-2,
pubmed-meshheading:17531811-Gene Silencing,
pubmed-meshheading:17531811-Genes, Reporter,
pubmed-meshheading:17531811-HeLa Cells,
pubmed-meshheading:17531811-Humans,
pubmed-meshheading:17531811-Kidney,
pubmed-meshheading:17531811-Neoplasm Proteins,
pubmed-meshheading:17531811-RNA, Messenger,
pubmed-meshheading:17531811-RNA Interference,
pubmed-meshheading:17531811-Recombinant Fusion Proteins,
pubmed-meshheading:17531811-Transfection
|
pubmed:year |
2007
|
pubmed:articleTitle |
RNA helicase A interacts with RISC in human cells and functions in RISC loading.
|
pubmed:affiliation |
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|