Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5658
pubmed:dateCreated
2004-1-30
pubmed:abstractText
Genes normally resident in euchromatic domains are silenced when packaged into heterochromatin, as exemplified in Drosophila melanogaster by position effect variegation (PEV). Loss-of-function mutations resulting in suppression of PEV have identified critical components of heterochromatin, including proteins HP1, HP2, and histone H3 lysine 9 methyltransferase. Here, we demonstrate that this silencing is dependent on the RNA interference machinery, using tandem mini-white arrays and white transgenes in heterochromatin to show loss of silencing as a result of mutations in piwi, aubergine, or spindle-E (homeless), which encode RNAi components. These mutations result in reduction of H3 Lys9 methylation and delocalization of HP1 and HP2, most dramatically in spindle-E mutants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Argonaute Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heterochromatin, http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Induced Silencing Complex, http://linkedlifedata.com/resource/pubmed/chemical/heterochromatin protein 1..., http://linkedlifedata.com/resource/pubmed/chemical/piwi protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/spindle E protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/white protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
30
pubmed:volume
303
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-72
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:14752161-ATP-Binding Cassette Transporters, pubmed-meshheading:14752161-Adenosine Triphosphatases, pubmed-meshheading:14752161-Alleles, pubmed-meshheading:14752161-Animals, pubmed-meshheading:14752161-Argonaute Proteins, pubmed-meshheading:14752161-Chromosomal Proteins, Non-Histone, pubmed-meshheading:14752161-Drosophila Proteins, pubmed-meshheading:14752161-Drosophila melanogaster, pubmed-meshheading:14752161-Eye Proteins, pubmed-meshheading:14752161-Gene Silencing, pubmed-meshheading:14752161-Genes, Insect, pubmed-meshheading:14752161-Heterochromatin, pubmed-meshheading:14752161-Histone-Lysine N-Methyltransferase, pubmed-meshheading:14752161-Histones, pubmed-meshheading:14752161-Methylation, pubmed-meshheading:14752161-Mutation, pubmed-meshheading:14752161-Proteins, pubmed-meshheading:14752161-RNA Interference, pubmed-meshheading:14752161-RNA-Induced Silencing Complex, pubmed-meshheading:14752161-Transgenes
pubmed:year
2004
pubmed:articleTitle
Heterochromatic silencing and HP1 localization in Drosophila are dependent on the RNAi machinery.
pubmed:affiliation
Division of Biological Sciences, 117 Tucker Hall, University of Missouri, Columbia, MO 65211, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't