pubmed-article:19651888 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C2754752 | lld:lifeskim |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C0242850 | lld:lifeskim |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:19651888 | lifeskim:mentions | umls-concept:C1956352 | lld:lifeskim |
pubmed-article:19651888 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:19651888 | pubmed:dateCreated | 2009-8-11 | lld:pubmed |
pubmed-article:19651888 | pubmed:abstractText | Nuage, a well-conserved perinuclear organelle found in germline cells, is thought to mediate retroelement repression in Drosophila melanogaster by regulating the production of Piwi-interacting RNAs (piRNAs). In this study, we present evidence that the nuage-piRNA pathway components can be found in cytoplasmic foci that also contain retroelement transcripts, antisense piRNAs, and proteins involved in messenger RNA (mRNA) degradation. These mRNA degradation proteins, decapping protein 1/2 (DCP1/2), Me31B (maternal expression at 31B), and pacman (PCM), are normally thought of as components of processing bodies. In spindle-E (spn-E) and aubergine (aub) mutants that lack piRNA production, piRNA pathway proteins no longer overlap the mRNA degradation proteins. Concomitantly, spn-E and aub mutant ovaries show an accumulation of full-length retroelement transcripts and prolonged stabilization of HeT-A mRNA, supporting the role of piRNAs in mediating posttranscriptional retroelement silencing. HeT-A mRNA is derepressed in mRNA degradation mutants twin, dcp1, and ski3, indicating that these enzymes also aid in removing full-length transcripts and/or decay intermediates. | lld:pubmed |
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pubmed-article:19651888 | pubmed:language | eng | lld:pubmed |
pubmed-article:19651888 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19651888 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19651888 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19651888 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19651888 | pubmed:month | Aug | lld:pubmed |
pubmed-article:19651888 | pubmed:issn | 1540-8140 | lld:pubmed |
pubmed-article:19651888 | pubmed:author | pubmed-author:KaiToshieT | lld:pubmed |
pubmed-article:19651888 | pubmed:author | pubmed-author:LimAi KhimAK | lld:pubmed |
pubmed-article:19651888 | pubmed:author | pubmed-author:TaoLihengL | lld:pubmed |
pubmed-article:19651888 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19651888 | pubmed:day | 10 | lld:pubmed |
pubmed-article:19651888 | pubmed:volume | 186 | lld:pubmed |
pubmed-article:19651888 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19651888 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19651888 | pubmed:pagination | 333-42 | lld:pubmed |
pubmed-article:19651888 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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