A HIGHLY CONSERVED DOMAIN OF TFIID DISPLAYS SPECIES SPECIFICITY INVIVO

被引：86

作者：

GILL, G ^{[1
]}

TJIAN, R ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT MOLEC & CELL BIOL,BERKELEY,CA 94720

来源：

CELL | 1991年 / 65卷 / 02期

关键词：

D O I：

10.1016/0092-8674(91)90166-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recombinant TFIID proteins from yeast, Drosophila, and human function interchangeably in vitro to restore basal level transcription to a human HeLa extract depleted for TFIID. Here we report that the recently cloned human and Drosophila TFIID genes fail to substitute in vivo for the S. cerevisiae TFIID gene, SPT15, which is essential for viability. Analysis of yeast-human hybrid TFIID proteins reveals that the failure of human TFIID to functionally replace yeast TFIID maps to the highly conserved C-terminal domain. Thus, the C-terminal conserved domain of TFIID, as well as the N-terminal divergent domain, appears to be involved in species-specific interactions.

引用

页码：333 / 340

页数：8

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