| pubmed-article:10882077 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0001068 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0162493 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C1425187 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C2613318 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0013057 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0066686 | lld:lifeskim |
| pubmed-article:10882077 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:10882077 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10882077 | pubmed:dateCreated | 2000-7-17 | lld:pubmed |
| pubmed-article:10882077 | pubmed:abstractText | Dosage compensation in Drosophila involves a 2-fold increase in transcription from the single male X relative to the two female X chromosomes. Regulation at the level of the chromosome involves alterations in chromatin organization: male X chromosomes appear decondensed and are marked by acetylation of histone H4 at lysine 16. We demonstrate that MOF, a protein required for dosage compensation with significant sequence similarity to the MYST family of acetyltransferases, is a histone acetyltransferase that acetylates chromatin specifically at histone H4 lysine 16. This acetylation relieves chromatin-mediated repression of transcription in vitro and in vivo if MOF is targeted to a promoter by fusion to a DNA-binding domain. Acetylation of chromatin by MOF, therefore, appears to be causally involved in transcriptional activation during dosage compensation. | lld:pubmed |
| pubmed-article:10882077 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10882077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10882077 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10882077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10882077 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10882077 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10882077 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:10882077 | pubmed:author | pubmed-author:AkhtarAA | lld:pubmed |
| pubmed-article:10882077 | pubmed:author | pubmed-author:BeckerP BPB | lld:pubmed |
| pubmed-article:10882077 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10882077 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:10882077 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10882077 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10882077 | pubmed:pagination | 367-75 | lld:pubmed |
| pubmed-article:10882077 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:10882077 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10882077 | pubmed:articleTitle | Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. | lld:pubmed |
| pubmed-article:10882077 | pubmed:affiliation | The Gene Expression Programme, European Molecular Biology Laboratory, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:10882077 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10882077 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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