Source:http://linkedlifedata.com/resource/pubmed/id/12711307
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-4-24
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pubmed:abstractText |
Interferon regulatory factor-1 (IRF-1), a putative tumor suppressor protein, is a transcriptional mediator of interferon-responsive signaling pathways that are involved in antiviral defense, apoptosis, immune response, and cell growth regulation. To delineate the IRF-1 domain responsible for transactivation, we performed a detailed deletion analysis of IRF-1. We found that the amino acid segment 217-260 was necessary and sufficient for transactivation. The structure of this region was predicted to be loop-helix-loop-sheet using the program PHD. Further studies indicated that casein kinase II and protein kinase C sites on each of the two loops are not important for transactivation, and a region containing amino acids 233-255 comprises the core activation domain. To verify the physiological role of segment 233-255, we constructed an IRF-1 deletion mutant lacking these amino acids and examined it using IRF-1 transactivation assay, fluorescence-activated cell sorting, and in situ beta-galactosidase staining techniques. From the results of these studies, we conclude that the amino acid segment 233-255 of IRF-1 comprises the core activation domain required for the physiological functions of IRF-1.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/IRF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Regulatory Factor-1,
http://linkedlifedata.com/resource/pubmed/chemical/Irf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
304
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12711307-3T3 Cells,
pubmed-meshheading:12711307-Animals,
pubmed-meshheading:12711307-DNA-Binding Proteins,
pubmed-meshheading:12711307-Humans,
pubmed-meshheading:12711307-Interferon Regulatory Factor-1,
pubmed-meshheading:12711307-Mice,
pubmed-meshheading:12711307-Mutagenesis, Site-Directed,
pubmed-meshheading:12711307-Phosphoproteins,
pubmed-meshheading:12711307-Protein Structure, Tertiary,
pubmed-meshheading:12711307-Sequence Deletion,
pubmed-meshheading:12711307-Trans-Activators,
pubmed-meshheading:12711307-Transcriptional Activation,
pubmed-meshheading:12711307-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Functional dissection of the transactivation domain of interferon regulatory factor-1.
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pubmed:affiliation |
Department of Bioscience and Biotechnology/Institute of Bioscience, Sejong University, 98 Kunja-dong, Kwangjin-gu, Seoul 143-747, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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