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

被引：190

作者：

QURESHI, SA ^{[1
]}

SALDITTGEORGIEFF, M ^{[1
]}

DARNELL, JE ^{[1
]}

机构：

[1] ROCKEFELLER UNIV,MOLEC CELL BIOL LAB,NEW YORK,NY 10021

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 09期

关键词：

D O I：

10.1073/pnas.92.9.3829

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Interferon a induction of transcription operates through interferon-stimulated-gene factor 3 (ISGF), a transcription factor two components of which are members of the newly characterized Stat family of transcription factors. Interferon alpha induces tyrosine phosphorylation of Stat1 and Stat2 proteins that associate and, together with a 48-kDa protein, 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 interferon-stimulated response element, the binding site of the ISGF3.

引用

页码：3829 / 3833

页数：5

共 23 条

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