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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6861
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pubmed:dateCreated |
2001-11-19
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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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/Codon, Nonsense,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
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/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
414
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-83
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11713521-Amino Acid Sequence,
pubmed-meshheading:11713521-Animals,
pubmed-meshheading:11713521-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:11713521-Chromosome Mapping,
pubmed-meshheading:11713521-Chromosomes, Fungal,
pubmed-meshheading:11713521-Codon, Nonsense,
pubmed-meshheading:11713521-DNA, Fungal,
pubmed-meshheading:11713521-DNA Methylation,
pubmed-meshheading:11713521-Eukaryotic Cells,
pubmed-meshheading:11713521-Gene Expression Regulation, Fungal,
pubmed-meshheading:11713521-Gene Silencing,
pubmed-meshheading:11713521-Heterochromatin,
pubmed-meshheading:11713521-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:11713521-Histones,
pubmed-meshheading:11713521-Lysine,
pubmed-meshheading:11713521-Methyltransferases,
pubmed-meshheading:11713521-Molecular Sequence Data,
pubmed-meshheading:11713521-Neurospora crassa,
pubmed-meshheading:11713521-Open Reading Frames,
pubmed-meshheading:11713521-Protein Methyltransferases,
pubmed-meshheading:11713521-Protein Structure, Tertiary,
pubmed-meshheading:11713521-Proteins,
pubmed-meshheading:11713521-Sequence Alignment,
pubmed-meshheading:11713521-Signal Transduction,
pubmed-meshheading:11713521-Transcription Factors,
pubmed-meshheading:11713521-Transgenes
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pubmed:year |
2001
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pubmed:articleTitle |
A histone H3 methyltransferase controls DNA methylation in Neurospora crassa.
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pubmed:affiliation |
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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