H4 acetylation does not replace H3 acetylation in chromatin remodelling and transcription activation of Adr1-dependent genes

被引:27
作者
Agricola, Eleonora
Verdone, Loredana
Di Mauro, Ernesto
Caserta, Micaela [1 ]
机构
[1] CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy
[2] Univ Roma La Sapienza, Dipartimento Genet & Biol Mol, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy
关键词
D O I
10.1111/j.1365-2958.2006.05451.x
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
Histone acetylation regulates gene expression. Whether this is caused by a general increase in nucleosome fluidity due to charge neutralization or by a more specific code is still matter of debate. By using a set of glucose-repressed Adr1-dependent genes of Saccharomyces cerevisiae, whose transcription was previously shown to require both Gcn5 and Esa1, we asked how changes of histone acetylation patterns at the promoter nucleosomes regulate chromatin remodelling and activation. When the signal of glucose reduction reaches the cells, H4 acetylation is kept constant while an increase of H3 acetylation occurs, in an Adr1- and Gcn5-dependent manner. In cells lacking Gcn5 activity, the H3 acetylation increase does not occur and an unexpected increase of histone H4 acetylation is observed. Nevertheless, chromatin remodelling and transcription activation are impaired, suggesting that acetylation of H3 and H4 histones plays different roles.
引用
收藏
页码:1433 / 1446
页数:14
相关论文
共 61 条
[1]   Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions [J].
Adkins, MW ;
Tyler, JK .
MOLECULAR CELL, 2006, 21 (03) :405-416
[2]   Common chromatin architecture, common chromatin remodeling, and common transcription kinetics of Adr1-dependent genes in Saccharomyces cerevisiae [J].
Agricola, E ;
Verdone, L ;
Xella, B ;
Di Mauro, E ;
Caserta, M .
BIOCHEMISTRY, 2004, 43 (27) :8878-8884
[3]   Multiple mechanistically distinct functions of SAGA at the PH05 promoter [J].
Barbaric, S ;
Reinke, H ;
Hörz, W .
MOLECULAR AND CELLULAR BIOLOGY, 2003, 23 (10) :3468-3476
[4]   Histone modifications in transcriptional regulation [J].
Berger, SL .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 2002, 12 (02) :142-148
[5]   Nucleosomes unfold completely at a transcriptionally active promoter [J].
Boeger, H ;
Griesenbeck, J ;
Strattan, JS ;
Kornberg, RD .
MOLECULAR CELL, 2003, 11 (06) :1587-1598
[6]   Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes [J].
Brower-Toland, B ;
Wacker, DA ;
Fulbright, RM ;
Lis, JT ;
Kraus, WL ;
Wang, MD .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 346 (01) :135-146
[7]   Independent recruitment in vivo by Gal4 of two complexes required for transcription [J].
Bryant, GO ;
Ptashne, M .
MOLECULAR CELL, 2003, 11 (05) :1301-1309
[8]   Ordered recruitment: Gene-specific mechanism of transcription activation [J].
Cosma, MP .
MOLECULAR CELL, 2002, 10 (02) :227-236
[9]   Histone acetylation at promoters is differentially affected by specific activators and repressors [J].
Deckert, J ;
Struhl, K .
MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (08) :2726-2735
[10]   Structure and ligand of a histone acetyltransferase bromodomain [J].
Dhalluin, C ;
Carlson, JE ;
Zeng, L ;
He, C ;
Aggarwal, AK ;
Zhou, MM .
NATURE, 1999, 399 (6735) :491-496