Source:http://linkedlifedata.com/resource/pubmed/id/19741270
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
47
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pubmed:dateCreated |
2009-11-16
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pubmed:abstractText |
Gene transcription in eukaryotes is modulated by the coordinated recruitment of specific transcription factors and chromatin-modulating proteins. Indeed, gene activation and/or repression is/are regulated by histone methylation status at specific arginine or lysine residues. In this work, by co-immunoprecipitation experiments, we demonstrate that PRMT5, a type II protein arginine methyltransferase that monomethylates and symmetrically dimethylates arginine residues, is physically associated with the Kruppel-like associated box-zinc finger protein ZNF224, the aldolase A gene repressor. Moreover, chromatin immunoprecipitation assays show that PRMT5 is recruited to the L-type aldolase A promoter and that methylation of the nucleosomes that surround the L-type promoter region occurs in vivo on the arginine 3 of histone H4. Consistent with its association to the ZNF224 repressor complex, the decrease of PRMT5 expression produced by RNA interference positively affects L-type aldolase A promoter transcription. Finally, the alternating occupancy of the L-type aldolase A promoter by the ZNF224-PRMT5 repression complex in proliferating and growth-arrested cells suggests that these regulatory proteins play a significant role during the cell cycle modulation of human aldolase A gene expression. Our data represent the first experimental evidence that protein arginine methylation plays a role in ZNF224-mediated transcriptional repression and provide novel insight into the chromatin modifications required for repression of gene transcription by Kruppel-like associated box-zinc finger proteins.
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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/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose-Bisphosphate Aldolase,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/PRMT5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ZNF224 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32321-30
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pubmed:dateRevised |
2011-3-3
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pubmed:meshHeading |
pubmed-meshheading:19741270-Arginine,
pubmed-meshheading:19741270-Cell Line,
pubmed-meshheading:19741270-Chromatin,
pubmed-meshheading:19741270-Chromatin Immunoprecipitation,
pubmed-meshheading:19741270-Flow Cytometry,
pubmed-meshheading:19741270-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:19741270-Gene Deletion,
pubmed-meshheading:19741270-Histones,
pubmed-meshheading:19741270-Humans,
pubmed-meshheading:19741270-Methylation,
pubmed-meshheading:19741270-Mutation,
pubmed-meshheading:19741270-Protein Methyltransferases,
pubmed-meshheading:19741270-Repressor Proteins,
pubmed-meshheading:19741270-Transcription, Genetic,
pubmed-meshheading:19741270-Zinc Fingers
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pubmed:year |
2009
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pubmed:articleTitle |
The Kruppel-like zinc finger protein ZNF224 recruits the arginine methyltransferase PRMT5 on the transcriptional repressor complex of the aldolase A gene.
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pubmed:affiliation |
Dipartimento di Biochimica e Biotecnologie Mediche, Università di Napoli Federico II, Via S. Pansini 5, Napoli 80131, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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