| pubmed-article:11713521 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11713521 | lifeskim:mentions | umls-concept:C0027923 | lld:lifeskim |
| pubmed-article:11713521 | lifeskim:mentions | umls-concept:C0376452 | lld:lifeskim |
| pubmed-article:11713521 | lifeskim:mentions | umls-concept:C0062776 | lld:lifeskim |
| pubmed-article:11713521 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:11713521 | pubmed:issue | 6861 | lld:pubmed |
| pubmed-article:11713521 | pubmed:dateCreated | 2001-11-19 | lld:pubmed |
| pubmed-article:11713521 | pubmed:abstractText | DNA methylation is involved in epigenetic processes such as X-chromosome inactivation, imprinting and silencing of transposons. We have demonstrated previously that dim-2 encodes a DNA methyltransferase that is responsible for all known cytosine methylation in Neurospora crassa. Here we report that another Neurospora gene, dim-5, is required for DNA methylation, as well as for normal growth and full fertility. We mapped dim-5 and identified it by transformation with a candidate gene. The mutant has a nonsense mutation in a SET domain of a gene related to histone methyltransferases that are involved in heterochromatin formation in other organisms. Transformation of a wild-type strain with a segment of dim-5 reactivated a silenced hph gene, apparently by 'quelling' of dim-5. We demonstrate that recombinant DIM-5 protein specifically methylates histone H3 and that replacement of lysine 9 in histone H3 with either a leucine or an arginine phenocopies the dim-5 mutation. We conclude that DNA methylation depends on histone methylation. | lld:pubmed |
| pubmed-article:11713521 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11713521 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11713521 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11713521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11713521 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11713521 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:11713521 | pubmed:author | pubmed-author:SelkerE UEU | lld:pubmed |
| pubmed-article:11713521 | pubmed:author | pubmed-author:TamaruHH | lld:pubmed |
| pubmed-article:11713521 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11713521 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11713521 | pubmed:volume | 414 | lld:pubmed |
| pubmed-article:11713521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11713521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11713521 | pubmed:pagination | 277-83 | lld:pubmed |
| pubmed-article:11713521 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11713521 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11713521 | pubmed:articleTitle | A histone H3 methyltransferase controls DNA methylation in Neurospora crassa. | lld:pubmed |
| pubmed-article:11713521 | pubmed:affiliation | Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA. | lld:pubmed |
| pubmed-article:11713521 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11713521 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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