Source:http://linkedlifedata.com/resource/pubmed/id/17825834
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-10-1
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pubmed:abstractText |
The BRAHMA (BRM) gene encodes the SNF2-type ATPase of the putative Arabidopsis thaliana SWI/SNF chromatin remodelling complex. This family of ATPases is characterized by the presence of a conserved catalytic domain and an arrangement of auxiliary domains, whose functions in the remodelling activity remains unclear. Here, we characterize, at the molecular and functional level, the carboxy-terminal part of Arabidopsis BRM. We have found three DNA-binding regions that bind various free DNA and nucleosomal probes with different specificity. One of these regions contains an AT-hook motif. The carboxy terminus also contains a bromodomain able to bind histones H3 and H4. We propose that this array of domains constitute a nucleosome interaction module that helps BRM to interact with its substrate. We also characterize an Arabidopsis mutant that expresses a BRM protein lacking the last 454 amino acid residues (BRM-DeltaC), encompassing the bromodomain and two of the three DNA-binding activities identified. This mutant displays an intermediate phenotype between those of the wild-type and a null allele mutant, suggesting that the nucleosome interaction module is required for the normal function of BRM but it is not essential for the remodelling activity of BRM-containing SWI/SNF complexes.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BRM protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/T-DNA
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
373
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
240-50
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pubmed:meshHeading |
pubmed-meshheading:17825834-Adenosine Triphosphatases,
pubmed-meshheading:17825834-Amino Acid Sequence,
pubmed-meshheading:17825834-Arabidopsis,
pubmed-meshheading:17825834-Arabidopsis Proteins,
pubmed-meshheading:17825834-Binding Sites,
pubmed-meshheading:17825834-DNA, Bacterial,
pubmed-meshheading:17825834-DNA, Plant,
pubmed-meshheading:17825834-Flowers,
pubmed-meshheading:17825834-Genes, Plant,
pubmed-meshheading:17825834-Histones,
pubmed-meshheading:17825834-Molecular Sequence Data,
pubmed-meshheading:17825834-Mutation,
pubmed-meshheading:17825834-Nucleosomes,
pubmed-meshheading:17825834-Protein Structure, Tertiary,
pubmed-meshheading:17825834-Recombinant Fusion Proteins,
pubmed-meshheading:17825834-Sequence Alignment
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pubmed:year |
2007
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pubmed:articleTitle |
A nucleosome interaction module is required for normal function of Arabidopsis thaliana BRAHMA.
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pubmed:affiliation |
Centro Andaluz de Biología Molecular y Medicina Regenerativa and Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas, Américo Vespucio s/n, E-41092 Sevilla, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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