TYROSINE-PHOSPHORYLATED STAT1 AND STAT2 PLUS A 48-KDA PROTEIN ALL CONTACT DNA IN FORMING INTERFERON-STIMULATED-GENE FACTOR-3

Citation
Sa. Qureshi et al., TYROSINE-PHOSPHORYLATED STAT1 AND STAT2 PLUS A 48-KDA PROTEIN ALL CONTACT DNA IN FORMING INTERFERON-STIMULATED-GENE FACTOR-3, Proceedings of the National Academy of Sciences of the United Statesof America, 92(9), 1995, pp. 3829-3833
Citations number
23
Categorie Soggetti
Multidisciplinary Sciences
ISSN journal
00278424
Volume
92
Issue
9
Year of publication
1995
Pages
3829 - 3833
Database
ISI
SICI code
0027-8424(1995)92:9<3829:TSASPA>2.0.ZU;2-6
Abstract
Interferon a induction of transcription operates through interferon-st imulated-gene factor 3 (ISGF), a transcription factor two components o f which are members of the newly characterized Stat family of transcri ption factors. Interferon alpha induces tyrosine phosphorylation of St at1 and Stat2 proteins that associate and, together with a 48-kDa prot ein, form ISGF3, Evidence is presented that a heterodimer of Stat1 and Stat2 is present in ISGF3 and that Stat1 and the 48-kDa protein make precise contact, while Stat2 makes general contact, with the interfero n-stimulated response element, the binding site of the ISGF3.