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Titolo:
Binding of HMG-I(Y) imparts architectural specificity to a positioned nucleosome on the promoter of the human interleukin-2 receptor alpha gene
Autore:
Reeves, R; Leonard, WJ; Nissen, MS;
Indirizzi:
Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Biosci, Pullman, WA 99164 USA NHLBI, Lab Mol Immunol, NIH, Bethesda, MD 20892 USA NHLBI Bethesda MD USA20892 Lab Mol Immunol, NIH, Bethesda, MD 20892 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 13, volume: 20, anno: 2000,
pagine: 4666 - 4679
SICI:
0270-7306(200007)20:13<4666:BOHIAS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROUP PROTEIN I/Y; DNA-BINDING; TRANSCRIPTIONAL ACTIVATORS; CHROMOSOMAL-PROTEINS; HISTONE OCTAMER; LINKER HISTONES; CHAIN PROMOTER; CHROMATIN; MOBILITY; ENHANCER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Reeves, R Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 ullman, WA 99164 USA
Citazione:
R. Reeves et al., "Binding of HMG-I(Y) imparts architectural specificity to a positioned nucleosome on the promoter of the human interleukin-2 receptor alpha gene", MOL CELL B, 20(13), 2000, pp. 4666-4679

Abstract

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 architecturaltranscription factor HMG-I(Y) cooperate in transcriptional regulation of the human IL-2R alpha 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 inthe 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-2R alphagene 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 tothe 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-2R alpha transcriptional activation in lymphocytes in vivo.

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Documento generato il 18/01/21 alle ore 13:59:17