Source:http://linkedlifedata.com/resource/pubmed/id/18498779
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6-7
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pubmed:dateCreated |
2008-6-23
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pubmed:abstractText |
Arabidopsis GCN5 is a major histone acetyltransferase. The mutation of the gene induces pleiotropic effects on plant development, and affects the expression of a large number of genes. The mechanism of action of this protein in controlling plant chromatin structure and genome expression is not understood. In this work, we report the identification of a number of potential protein interacting partners of GCN5 in Arabidopsis. In particular, GCN5 was shown to interact specifically with a phosphatase 2C protein (AtPP2C-6-6). GCN5 phosphorylated by activities in cellular extracts could be dephosphorylated by AtPP2C-6-6 in vitro. Analysis of T-DNA insertion mutants revealed a positive role of AtPP2C-6-6 in salt induction of stress-inducible genes, while the gcn5 mutation seemed to have no effect on the induction but showed up-regulation of a subset of the stress-inducible genes under non-induced conditions. In addition, the gcn5 mutation seriously reduced acetylation of histone H3K14 and H3K27, whereas the T-DNA insertions of the AtPP2C6-6 gene enhanced the acetylation of these lysine residues. Taken together, the present data suggest that AtPP2C-6-6 may function as a negative regulator of GCN5 activity in Arabidopsis.
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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/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/KAT2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1779
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
376-82
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pubmed:dateRevised |
2008-9-13
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pubmed:meshHeading |
pubmed-meshheading:18498779-Acetylation,
pubmed-meshheading:18498779-Arabidopsis,
pubmed-meshheading:18498779-Arabidopsis Proteins,
pubmed-meshheading:18498779-Gene Expression Regulation, Plant,
pubmed-meshheading:18498779-Genes, Plant,
pubmed-meshheading:18498779-Histone Acetyltransferases,
pubmed-meshheading:18498779-Histones,
pubmed-meshheading:18498779-Mutagenesis, Insertional,
pubmed-meshheading:18498779-Phosphoprotein Phosphatases,
pubmed-meshheading:18498779-Phosphorylation,
pubmed-meshheading:18498779-Phylogeny,
pubmed-meshheading:18498779-Protein Interaction Mapping,
pubmed-meshheading:18498779-Recombinant Proteins,
pubmed-meshheading:18498779-Two-Hybrid System Techniques
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pubmed:articleTitle |
Characterization of a phosphatase 2C protein as an interacting partner of the histone acetyltransferase GCN5 in Arabidopsis.
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pubmed:affiliation |
Institut de Biotechnologie des Plantes, CNRS UMR8618, Université Paris sud 11, 91405 Orsay, France.
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pubmed:publicationType |
Journal Article
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