A subset of TAFIIs are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation

被引：379
作者：
Grant, PA
Schieltz, D
Pray-Grant, MG
Steger, DJ
Reese, JC
Yates, JR
Workman, JL [1 ]
机构：
[1] Penn State Univ, Howard Hughes Med Inst, University Pk, PA 16802 USA
[2] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
[3] Univ Washington, Hlth Sci Ctr, Dept Mol Biotechnol, Seattle, WA 98195 USA
来源：
CELL | 1998年 / 94卷 / 01期
关键词：
D O I：
10.1016/S0092-8674(00)81220-9
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：
A number of transcriptional coactivator proteins have been identified as histone acetyltransferase (HAT) proteins, providing a direct molecular basis for the coupling of histone acetylation and transcriptional activation. The yeast Spt-Ada-Gcn5-acetyltransferase (SAGA) complex requires the coactivator protein Gcn5 for HAT activity. Identification of protein subunits by mass spectrometry and immunoblotting revealed that the TATA binding protein-associated factors (TAF(II)s) TAF(II)90, -68/61, -60, -25/23, and -20/17 are integral components of this complex. in addition, TAF(II)68 was required for both SAGA-dependent nucleosomal HAT activity and transcriptional activation from chromatin templates in vitro. These results illustrate a role for certain TAF(II) proteins in the regulation of gene expression at the level of chromatin modification that is distinct from the TFIID complex and TAF(II)145.
引用
收藏
页码：45 / 53
页数：9
相关论文
共 59 条
[11]   The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gcn5p coactivator complex [J].
Drysdale, CM ;
Jackson, BM ;
McVeigh, R ;
Klebanow, ER ;
Bai, Y ;
Kokubo, T ;
Swanson, M ;
Nakatani, Y ;
Weil, PA ;
Hinnebusch, AG .
MOLECULAR AND CELLULAR BIOLOGY, 1998, 18 (03) :1711-1724
[12]   Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4 [J].
Edmondson, DG ;
Smith, MM ;
Roth, SY .
GENES & DEVELOPMENT, 1996, 10 (10) :1247-1259
[13]   AN APPROACH TO CORRELATE TANDEM MASS-SPECTRAL DATA OF PEPTIDES WITH AMINO-ACID-SEQUENCES IN A PROTEIN DATABASE [J].
ENG, JK ;
MCCORMACK, AL ;
YATES, JR .
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 1994, 5 (11) :976-989
[14]   The nucleosomal array: Structure/function relationships [J].
Fletcher, TM ;
Hansen, JC .
CRITICAL REVIEWS IN EUKARYOTIC GENE EXPRESSION, 1996, 6 (2-3) :149-188
[15]  
GAITLIN CL, 1998, IN PRESS J ANAL BIOC
[16]   2 DISTINCT YEAST TRANSCRIPTIONAL ACTIVATORS REQUIRE THE FUNCTION OF THE GCN5 PROTEIN TO PROMOTE NORMAL LEVELS OF TRANSCRIPTION [J].
GEORGAKOPOULOS, T ;
THIREOS, G .
EMBO JOURNAL, 1992, 11 (11) :4145-4152
[17]   Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex [J].
Grant, PA ;
Duggan, L ;
Cote, J ;
Roberts, SM ;
Brownell, JE ;
Candau, R ;
Ohba, R ;
OwenHughes, T ;
Allis, CD ;
Winston, F ;
Berger, SL ;
Workman, JL .
GENES & DEVELOPMENT, 1997, 11 (13) :1640-1650
[18]   The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes [J].
Grant, PA ;
Sterner, DE ;
Duggan, LJ ;
Workman, JL ;
Berger, SL .
TRENDS IN CELL BIOLOGY, 1998, 8 (05) :193-197
[19]   HISTONE H3 AND H4 N-TERMINI INTERACT WITH SIR3 AND SIR4 PROTEINS - A MOLECULAR-MODEL FOR THE FORMATION OF HETEROCHROMATIN IN YEAST [J].
HECHT, A ;
LAROCHE, T ;
STRAHLBOLSINGER, S ;
GASSER, SM ;
GRUNSTEIN, M .
CELL, 1995, 80 (04) :583-592
[20]   A histone octamer-like structure within TFIID [J].
Hoffmann, A ;
Chiang, CM ;
Oelgeschlager, T ;
Xie, XL ;
Burley, SK ;
Nakatani, Y ;
Roeder, RG .
NATURE, 1996, 380 (6572) :356-359
123456