Molecular cloning and analysis of two subunits of the human TFIID complex: hTAF(II)130 and hTAF(II)100

被引:119
作者
Tanese, N
Saluja, D
Vassallo, MF
Chen, JL
Admon, A
机构
[1] NYU,MED CTR,KAPLAN CANC CTR,NEW YORK,NY 10016
[2] TULARIK INC,S SAN FRANCISCO,CA 94080
[3] TECHNION ISRAEL INST TECHNOL,DEPT BIOL,IL-32000 HAIFA,ISRAEL
关键词
D O I
10.1073/pnas.93.24.13611
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
Transcription factor TFIID is a multiprotein complex composed of the TATA box-binding protein (TBP) and multiple TBP-associated factors (TAFs), TFIID plays an essential role in mediating transcriptional activation by gene-specific activators, Numerous transcriptional activators have been characterized from mammalian cells; however, molecular analysis of the components of mammalian TFIID has been incomplete, Here we describe isolation of cDNAs encoding two TAF subunits of the human transcription factor TFIID, The first cDNA is predicted to encode the C-terminal 947 residues of the 130-kDa human TAF subunit, hTAF(II)130, The second cDNA encodes the C-terminal 801 residues of the 100-kDa subunit, hTAF(II)100. Recombinant TAFs expressed in human cells by transient transfections are capable of associating with the endogenous TAFs and TBP to form a TFIID complex in vivo. Protein binding experiments demonstrate that hTAF(II)130, like its Drosophila homolog dTAF(II)110, interacts with the glutamine-rich activation domains of the human transcription factor Spl. Furthermore, hTAF(II)130 shows reduced binding to the Spl mutants with impaired ability to activate transcription, suggesting a role for hTAF(II)130 as a direct coactivator target for Sp1.
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页码:13611 / 13616
页数:6
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