Source:http://linkedlifedata.com/resource/pubmed/id/12723697
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
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pubmed:dateCreated |
2003-5-1
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pubmed:abstractText |
Dosage compensation refers to the phenomenon that despite the difference in copy number of X chromosomes in males and females approximately equal expression results from the sex chromosomes. We describe evidence for a model that dosage compensation is caused by an 'inverse dosage effect' that results from an altered stoichiometry of transcriptional regulators on the X versus the autosomes. This imbalance of regulators would cause a two-fold increase in target gene expression throughout the genome in the absence of any modification. The two-fold hyperactivation compensates the X chromosome. However, the MSL (male specific lethal) complex modifies this effect on the autosomes, which would otherwise double their expression, by becoming sequestered to the X chromosome together with a histone acetylase (MOF) and kinase (JIL1). This situation reduces the level of histone 4 Lys16 acetylation and H3 phosphorylation on the autosomes, thus bringing their expression down to near the female level. The presence of the MSL complex on the X modifies chromatin in such a manner that it counteracts any impact of increased histone acetylation and phosphorylation on gene expression. This situation fosters the proper two-fold increase in gene expression needed for X chromosomal dosage compensation in males and reduces the inverse effect on the autosomes to equalize gene expression throughout the genome for the two sexes.
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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/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/mof protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0016-6707
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
179-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12723697-Acetyltransferases,
pubmed-meshheading:12723697-Animals,
pubmed-meshheading:12723697-Chromatin,
pubmed-meshheading:12723697-Dosage Compensation, Genetic,
pubmed-meshheading:12723697-Drosophila,
pubmed-meshheading:12723697-Drosophila Proteins,
pubmed-meshheading:12723697-Evolution, Molecular,
pubmed-meshheading:12723697-Histone Acetyltransferases,
pubmed-meshheading:12723697-Histones,
pubmed-meshheading:12723697-Male,
pubmed-meshheading:12723697-Nuclear Proteins,
pubmed-meshheading:12723697-Transcription, Genetic,
pubmed-meshheading:12723697-X Chromosome
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pubmed:year |
2003
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pubmed:articleTitle |
Dosage dependent gene regulation and the compensation of the X chromosome in Drosophila males.
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pubmed:affiliation |
University of Missouri, Columbia, 117 Tucker Hall, Columbia, MO 65211-7400, USA. BirchlerJ@Missouri.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Review
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