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rdf:type |
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lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0441655,
umls-concept:C0680022,
umls-concept:C1167142,
umls-concept:C1333892,
umls-concept:C1366355,
umls-concept:C1419813,
umls-concept:C1421934,
umls-concept:C1706171,
umls-concept:C1706172,
umls-concept:C1706603
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pubmed:issue |
3
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pubmed:dateCreated |
2001-7-16
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pubmed:abstractText |
Bicoid directs anterior development in Drosophila embryos by activating different genes along the anterior-posterior axis. However, its activity is down-regulated at the anterior tip of the embryo, in a process known as retraction. Retraction is under the control of the terminal polarity system, and results in localized repression of Bicoid target genes. Here, we describe a Drosophila homolog of human SAP18, a member of the Sin3A/Rpd3 histone deacetylase complex. dSAP18 interacts with Bicoid in yeast and in vitro, and is expressed early in development coincident with Bicoid. In tissue culture cells, dSAP18 inhibits the ability of Bicoid to activate reporter genes. These results suggest a model in which dSAP18 interacts with Bicoid to silence expression of Bicoid target genes in the anterior tip of the embryo.
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pubmed:grant |
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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/ATG16 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SAP18 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/bicoid interacting protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/bicoid protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0949-944X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
211
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
109-17
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pubmed:dateRevised |
2011-5-4
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pubmed:meshHeading |
pubmed-meshheading:11455422-Amino Acid Sequence,
pubmed-meshheading:11455422-Animals,
pubmed-meshheading:11455422-Base Sequence,
pubmed-meshheading:11455422-Carrier Proteins,
pubmed-meshheading:11455422-Chromosome Mapping,
pubmed-meshheading:11455422-DNA,
pubmed-meshheading:11455422-Drosophila,
pubmed-meshheading:11455422-Drosophila Proteins,
pubmed-meshheading:11455422-Gene Expression Regulation, Developmental,
pubmed-meshheading:11455422-Histone Deacetylases,
pubmed-meshheading:11455422-Homeodomain Proteins,
pubmed-meshheading:11455422-Humans,
pubmed-meshheading:11455422-Molecular Sequence Data,
pubmed-meshheading:11455422-Protein Binding,
pubmed-meshheading:11455422-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11455422-Sequence Homology, Amino Acid,
pubmed-meshheading:11455422-Trans-Activators,
pubmed-meshheading:11455422-Transcription, Genetic,
pubmed-meshheading:11455422-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
Drosophila SAP18, a member of the Sin3/Rpd3 histone deacetylase complex, interacts with Bicoid and inhibits its activity.
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pubmed:affiliation |
Molecular Genetics Program, Wadsworth Center, New York State Department of Health & Department of Biomedical Sciences, School of Public Health, State University of New York, Albany, NY 12208, USA. hanes@wadsworth.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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