Transcriptional activators direct histone acetyltransferase complexes to nucleosomes

被引:427
作者
Utley, RT
Ikeda, K
Grant, PA
Côté, J
Steger, DJ
Eberharter, A
John, S
Workman, JL [1 ]
机构
[1] Penn State Univ, Dept Biochem & Mol Biol, Howard Hughes Med Inst, University Pk, PA 16802 USA
[2] Penn State Univ, Ctr Gene Regulat, Althouse Lab 306, University Pk, PA 16802 USA
[3] Jichi Med Sch, Dept Biol, Minami Kawachi, Tochigi 32904, Japan
[4] Univ Laval, Hotel Dieu Quebec, Ctr Canc Res, Quebec City, PQ G1R 2J6, Canada
关键词
D O I
10.1038/28886
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
Transcriptional co-activators were originally identified as proteins that act as intermediaries between upstream activators and the basal transcription machinery. The discovery that co-activators such as Tetrahymena and yeast Gcn5( >)(1,2), as well as human p300/CBP3,4, pCAF(5), Src-1(6), ACTR(7) and TAFII250(8), can acetylate histones suggests that activators may be involved in targeting acetylation activity to promoters. Several histone deacetylases have been linked to transcriptional co-repressor proteins(9), suggesting that the action of both acetylases and deacetylases is important in the regulation of many genes. Here we demonstrate the binding of two native yeast histone acetyltransferase (HAT) complexes to the herpesvirus VP16 activation domain and the yeast transcriptional activator Gcn4 and show that it is their interaction with the VP16 activation domain that targets Gal4-VP16-bound nucleosomes for acetylation. We find that Gal4-VP16-driven transcription from chromatin templates is stimulated by both HAT complexes in an acetyl CoA-dependent reaction. Our results demonstrate the targeting of native HAT complexes by a transcription-activation domain to nucleosomes in order to activate transcription.
引用
收藏
页码:498 / 502
页数:5
相关论文
共 31 条
[1]   The CBP co-activator is a histone acetyltransferase [J].
Bannister, AJ ;
Kouzarides, T .
NATURE, 1996, 384 (6610) :641-643
[2]   CHARACTERIZATION OF PHYSICAL INTERACTIONS OF THE PUTATIVE TRANSCRIPTIONAL ADAPTER, ADA2, WITH ACIDIC ACTIVATION DOMAINS AND TATA-BINDING PROTEIN [J].
BARLEV, NA ;
CANDAU, R ;
WANG, LA ;
DARPINO, P ;
SILVERMAN, N ;
BERGER, SL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (33) :19337-19344
[3]   SELECTIVE-INHIBITION OF ACTIVATED BUT NOT BASAL TRANSCRIPTION BY THE ACIDIC ACTIVATION DOMAIN OF VP16 - EVIDENCE FOR TRANSCRIPTIONAL ADAPTERS [J].
BERGER, SL ;
CRESS, WD ;
CRESS, A ;
TRIEZENBERG, SJ ;
GUARENTE, L .
CELL, 1990, 61 (07) :1199-1208
[4]   GENETIC ISOLATION OF ADA2 - A POTENTIAL TRANSCRIPTIONAL ADAPTER REQUIRED FOR FUNCTION OF CERTAIN ACIDIC ACTIVATION DOMAINS [J].
BERGER, SL ;
PINA, B ;
SILVERMAN, N ;
MARCUS, GA ;
AGAPITE, J ;
REGIER, JL ;
TRIEZENBERG, SJ ;
GUARENTE, L .
CELL, 1992, 70 (02) :251-265
[5]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[6]   Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation [J].
Brownell, JE ;
Allis, CD .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 1996, 6 (02) :176-184
[7]   ACTIVATION OF YEAST POLYMERASE-II TRANSCRIPTION BY HERPESVIRUS VP16 AND GAL4 DERIVATIVES INVITRO [J].
CHASMAN, DI ;
LEATHERWOOD, J ;
CAREY, M ;
PTASHNE, M ;
KORNBERG, RD .
MOLECULAR AND CELLULAR BIOLOGY, 1989, 9 (11) :4746-4749
[8]   Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300 [J].
Chen, HW ;
Lin, RJ ;
Schiltz, RL ;
Chakravarti, D ;
Nash, A ;
Nagy, L ;
Privalsky, ML ;
Nakatani, Y ;
Evans, RM .
CELL, 1997, 90 (03) :569-580
[9]  
Cote J., 1995, METHODS MOL GENETICS, V6, P108
[10]   CRITICAL STRUCTURAL ELEMENTS OF THE VP16 TRANSCRIPTIONAL ACTIVATION DOMAIN [J].
CRESS, WD ;
TRIEZENBERG, SJ .
SCIENCE, 1991, 251 (4989) :87-90