pubmed-article:10848593 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C0905617 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C1101536 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C0028623 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C1537647 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:10848593 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:10848593 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:10848593 | pubmed:dateCreated | 2000-7-20 | lld:pubmed |
pubmed-article:10848593 | pubmed:abstractText | Transcriptional induction of the interleukin-2 receptor alpha-chain (IL-2Ralpha) gene is a key event regulating T-cell-mediated immunity in mammals. In vivo, the T-cell-restricted protein Elf-1 and the general architectural transcription factor HMG-I(Y) cooperate in transcriptional regulation of the human IL-2Ralpha gene by binding to a specific positive regulatory region (PRRII) in its proximal promoter. Employing chromatin reconstitution analyses, we demonstrate that the binding sites for both HMG-I(Y) and Elf-1 in the PRRII element are incorporated into a strongly positioned nucleosome in vitro. A variety of analytical techniques was used to determine that a stable core particle is positioned over most of the PRRII element and that this nucleosome exhibits only a limited amount of lateral translational mobility. Regardless of its translational setting, the in vitro position of the nucleosome is such that DNA recognition sequences for both HMG-I(Y) and Elf-1 are located on the surface of the core particle. Restriction nuclease accessibility analyses indicate that a similarly positioned nucleosome also exists on the PRRII element in unstimulated lymphocytes when the IL-2Ralpha gene is silent and suggest that this core particle is remodeled following transcriptional activation of the gene in vivo. In vitro experiments employing the chemical cleavage reagent 1,10-phenanthroline copper (II) covalently attached to its C-terminal end demonstrate that HMG-I(Y) protein binds to the positioned PRRII nucleosome in a direction-specific manner, thus imparting a distinct architectural configuration to the core particle. Together, these findings suggest a role for the HMG-I(Y) protein in assisting the remodeling of a critically positioned nucleosome on the PRRII promoter element during IL-2Ralpha transcriptional activation in lymphocytes in vivo. | lld:pubmed |
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pubmed-article:10848593 | pubmed:language | eng | lld:pubmed |
pubmed-article:10848593 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10848593 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10848593 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10848593 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10848593 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:10848593 | pubmed:author | pubmed-author:ReevesRR | lld:pubmed |
pubmed-article:10848593 | pubmed:author | pubmed-author:NissenM SMS | lld:pubmed |
pubmed-article:10848593 | pubmed:author | pubmed-author:LeonardW JWJ | lld:pubmed |
pubmed-article:10848593 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10848593 | pubmed:volume | 20 | lld:pubmed |
pubmed-article:10848593 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10848593 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10848593 | pubmed:pagination | 4666-79 | lld:pubmed |
pubmed-article:10848593 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10848593 | pubmed:meshHeading | pubmed-meshheading:10848593... | lld:pubmed |
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