Source:http://linkedlifedata.com/resource/pubmed/id/11739381
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
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| pubmed:dateCreated |
2002-2-11
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| pubmed:abstractText |
Nuclear factor (NF)-kappaB transcription factors are involved in the control of a large number of normal cellular and organismal processes, such as immune and inflammatory responses, developmental processes, cellular growth, and apoptosis. Transcription of the human immunodeficiency virus type 1 (HIV-1) genome depends on the intracellular environment where the integrate viral DNA is regulated by a complex interplay among viral regulatory proteins, such as Tat, and host cellular transcription factors, such as NF-kappaB, interacting with the viral long terminal repeat region. CBP (CREB-binding protein) and p300, containing an intrinsic histone acetyltransferase (HAT) activity, have emerged as coactivators for various DNA-binding transcription factors. Here, we show that the p50 subunit as well as the p50/p65 of NF-kappaB, and not other factors such as SP1, TFIIB, polymerase II, TFIIA, or p65, can be acetylated by CBP/p300 HAT domain. Acetylation of p50 was completely dependent on the presence of both HAT domain and Tat proteins, implying that Tat influences the transcription machinery by aiding CBP/p300 to acquire new partners and increase its functional repertoire. Three lysines, Lys-431, Lys-440, and Lys-441 in p50 were all acetylated in vitro, and a sequence similarity among p50, p53, Tat, and activin receptor type I on these particular lysines was observed. All proteins have been shown to be acetylated by the CBP/p300 HAT domain. Acetylated p50 increases its DNA binding properties, as evident by streptavidin/biotin pull-down assays when using labeled NF-kappaB oligonucleotides. Increased DNA binding on HIV-1 long terminal repeat coincided with increases in the rate of transcription. Therefore, we propose that acetylation of the DNA binding domain of NF-kappaB aids in nuclear translocation and enhanced transcription and also suggest that the substrate specificity of CBP/p300 can be altered by small peptide molecules, such as HIV-encoded Tat.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, tat,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B p50 Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelA,
http://linkedlifedata.com/resource/pubmed/chemical/tat Gene Products, Human...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
277
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
4973-80
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11739381-Acetylation,
pubmed-meshheading:11739381-Amino Acid Sequence,
pubmed-meshheading:11739381-Animals,
pubmed-meshheading:11739381-Cell Line,
pubmed-meshheading:11739381-Cells, Cultured,
pubmed-meshheading:11739381-DNA,
pubmed-meshheading:11739381-Dose-Response Relationship, Drug,
pubmed-meshheading:11739381-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11739381-Gene Products, tat,
pubmed-meshheading:11739381-Glutathione Transferase,
pubmed-meshheading:11739381-HIV-1,
pubmed-meshheading:11739381-Humans,
pubmed-meshheading:11739381-Insects,
pubmed-meshheading:11739381-Lysine,
pubmed-meshheading:11739381-Mass Spectrometry,
pubmed-meshheading:11739381-Molecular Sequence Data,
pubmed-meshheading:11739381-NF-kappa B,
pubmed-meshheading:11739381-NF-kappa B p50 Subunit,
pubmed-meshheading:11739381-Nuclear Proteins,
pubmed-meshheading:11739381-Plasmids,
pubmed-meshheading:11739381-Protein Binding,
pubmed-meshheading:11739381-Protein Structure, Tertiary,
pubmed-meshheading:11739381-Recombinant Fusion Proteins,
pubmed-meshheading:11739381-Sequence Homology, Amino Acid,
pubmed-meshheading:11739381-Trans-Activators,
pubmed-meshheading:11739381-Transcription, Genetic,
pubmed-meshheading:11739381-Transcription Factor RelA,
pubmed-meshheading:11739381-tat Gene Products, Human Immunodeficiency Virus
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| pubmed:year |
2002
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| pubmed:articleTitle |
Enhancement of nuclear factor-kappa B acetylation by coactivator p300 and HIV-1 Tat proteins.
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| pubmed:affiliation |
Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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