The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators

被引:147
作者
Lee, DY
Ezhkova, E
Li, B
Pattenden, SG
Tansey, WP
Workman, JL
机构
[1] Cold Spring Harbor Lab, Cold Spring Harbor, NY 11724 USA
[2] Stowers Inst Med Res, Kansas City, MO 64110 USA
[3] Watson Sch Biol Sci, Cold Spring Harbor, NY 11724 USA
关键词
D O I
10.1016/j.cell.2005.08.015
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
Promoter recruitment of the Saccharomyces cerevisiae SAGA histone acetyltransferase complex is required for RNA polymerase II-dependent transcription of several genes. SAGA is targeted to promoters through interactions with sequence-specific DNA binding transcriptional activators and facilitates preinitiation-complex assembly and transcription. Here, we show that the 19S proteasome regulatory particle (19S RP) alters SAGA to stimulate its interaction with transcriptional activators. The ATPase components of the 19S RP are required for stimulation of SAGA/activator interactions and enhance SAGA recruitment to promoters. Proteasomal ATPases genetically interact with SAGA, and their inhibition reduces global histone H3 acetylation levels and SAGA recruitment to target promoters in vivo. These results indicate that the 19S RIP modulates SAGA complex using its ATPase components, thereby facilitating subsequent transcription events at promoters.
引用
收藏
页码:423 / 436
页数:14
相关论文
共 54 条
[31]   Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome [J].
Navon, A ;
Goldberg, AL .
MOLECULAR CELL, 2001, 8 (06) :1339-1349
[32]   Activation domain-mediated targeting of the SWI/SNF complex to promoters stimulates transcription from nucleosome arrays [J].
Neely, KE ;
Hassan, AH ;
Wallberg, AE ;
Steger, DJ ;
Cairns, BR ;
Wright, APH ;
Workman, JL .
MOLECULAR CELL, 1999, 4 (04) :649-655
[33]  
Neuwald AF, 1999, GENOME RES, V9, P27
[34]   Targeted recruitment of set1 histone methylase by elongating pol II provides a localized mark and memory of recent transcriptional activity [J].
Ng, HH ;
Robert, F ;
Young, RA ;
Struhl, K .
MOLECULAR CELL, 2003, 11 (03) :709-719
[35]   The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway [J].
Pray-Grant, MG ;
Schieltz, D ;
McMahon, SJ ;
Wood, JM ;
Kennedy, EL ;
Cook, RG ;
Workman, JL ;
Yates, JR ;
Grant, PA .
MOLECULAR AND CELLULAR BIOLOGY, 2002, 22 (24) :8774-8786
[36]   Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation [J].
Pray-Grant, MG ;
Daniel, JA ;
Schieltz, D ;
Yates, JR ;
Grant, PA .
NATURE, 2005, 433 (7024) :434-438
[37]   Global position and recruitment of HATs and HDACs in the yeast genome [J].
Robert, F ;
Pokholok, DK ;
Hannett, NM ;
Rinaldi, NJ ;
Chandy, M ;
Rolfe, A ;
Workman, JL ;
Gifford, DK ;
Young, RA .
MOLECULAR CELL, 2004, 16 (02) :199-209
[38]   Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery [J].
Rodríguez-Navarro, S ;
Fischer, T ;
Luo, MJ ;
Antúnez, O ;
Brettschneider, S ;
Lechner, J ;
Pérez-Ortín, JE ;
Reed, R ;
Hurt, E .
CELL, 2004, 116 (01) :75-86
[39]   Active genes are tri-methylated at K4 of histone H3 [J].
Santos-Rosa, H ;
Schneider, R ;
Bannister, AJ ;
Sherriff, J ;
Bernstein, BE ;
Emre, NCT ;
Schreiber, SL ;
Mellor, J ;
Kouzarides, T .
NATURE, 2002, 419 (6905) :407-411
[40]   Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae [J].
Sone, T ;
Saeki, Y ;
Toh-e, A ;
Yokosawa, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (27) :28807-28816