Distinct contributions of MSL complex subunits to the transcriptional enhancement responsible for dosage compensation in Drosophila

被引:15
作者
Dunlap, David [1 ]
Yokoyama, Ruth [2 ]
Ling, Huiping [2 ]
Sun, He-Ying [2 ]
McGill, Kerry [1 ]
Cugusi, Simona [2 ]
Lucchesi, John C. [2 ]
机构
[1] Emory Univ, Dept Cell Biol, Atlanta, GA 30322 USA
[2] Emory Univ, Dept Biol, Atlanta, GA 30322 USA
基金
美国国家卫生研究院;
关键词
ORDER CHROMATIN-STRUCTURE; NUCLEOSOME CORE PARTICLE; REMODELING ATPASE ISWI; H4 TAIL ACETYLATIONS; X-CHROMOSOME; IN-VIVO; HISTONE ACETYLATION; H4-K16; ACETYLATION; ANALYSIS REVEALS; GENE-EXPRESSION;
D O I
10.1093/nar/gks890
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
The regulatory mechanism of dosage compensation is the paramount example of epigenetic regulation at the chromosomal level. In Drosophila, this mechanism, designed to compensate for the difference in the dosage of X-linked genes between the sexes, depends on the MSL complex that enhances the transcription of the single dose of these genes in males. We have investigated the function of various subunits of the complex in mediating dosage compensation. Our results confirm that the highly enriched specific acetylation of histone H4 at lysine 16 of compensated genes by the histone acetyl transferase subunit MOF induces a more disorganized state of their chromatin. We have determined that the association of the MSL complex reduces the level of negative supercoiling of the deoxyribonucleic acid of compensated genes, and we have defined the role that the other subunits of the complex play in this topological modification. Lastly, we have analyzed the potential contribution of ISWI-containing remodeling complexes to the architecture of compensated chromatin, and we suggest a role for this remodeling factor in dosage compensation.
引用
收藏
页码:11281 / 11291
页数:11
相关论文
共 64 条
[1]   High-resolution ChIP-chip analysis reveals that the Drosophila MSL complex selectively identifies active genes on the male X chromosome [J].
Alekseyenko, AA ;
Larschan, E ;
Lai, WR ;
Park, PJ ;
Kuroda, MI .
GENES & DEVELOPMENT, 2006, 20 (07) :848-857
[2]   A sequence motif within chromatin entry sites directs MSL establishment on the Drosophila X chromosome [J].
Alekseyenko, Artyom A. ;
Peng, Shouyong ;
Larschan, Erica ;
Gorchakov, Andrey A. ;
Lee, Ok-Kyung ;
Kharchenko, Peter ;
McGrath, Sean D. ;
Wang, Charlotte I. ;
Mardis, Elaine R. ;
Park, Peter J. ;
Kuroda, Mitzi I. .
CELL, 2008, 134 (04) :599-609
[3]   The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association [J].
Allahverdi, Abdollah ;
Yang, Renliang ;
Korolev, Nikolay ;
Fan, Yanping ;
Davey, Curt A. ;
Liu, Chuan-Fa ;
Nordenskioeld, Lars .
NUCLEIC ACIDS RESEARCH, 2011, 39 (05) :1680-1691
[4]   Regional control of chromatin organization by noncoding roX RNAs and the NURF remodeling complex in Drosophila melanogaster [J].
Bai, X. ;
Larschan, E. ;
Kwon, S. Y. ;
Badenhorst, P. ;
Kurodat, M. I. .
GENETICS, 2007, 176 (03) :1491-1499
[5]   Expression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexes [J].
Barrios, Adam ;
Selleck, William ;
Hnatkovich, Brian ;
Kramer, Ryan ;
Sermwittayawong, Decha ;
Tan, Song .
METHODS, 2007, 41 (03) :271-277
[6]   Accessibility of the Drosophila genome discriminates PcG repression, H4K16 acetylation and replication timing [J].
Bell, Oliver ;
Schwaiger, Michaela ;
Oakeley, Edward J. ;
Lienert, Florian ;
Beisel, Christian ;
Stadler, Michael B. ;
Schuebeler, Dirk .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2010, 17 (07) :894-U1
[7]   Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA [J].
Brower-Toland, BD ;
Smith, CL ;
Yeh, RC ;
Lis, JT ;
Peterson, CL ;
Wang, MD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (04) :1960-1965
[8]   ENTROPIC ELASTICITY OF LAMBDA-PHAGE DNA [J].
BUSTAMANTE, C ;
MARKO, JF ;
SIGGIA, ED ;
SMITH, S .
SCIENCE, 1994, 265 (5178) :1599-1600
[9]   The Drosophila NURF remodelling and the ATAC histone acetylase complexes functionally interact and are required for global chromosome organization [J].
Carre, Clement ;
Ciurciu, Anita ;
Komonyi, Orban ;
Jacquier, Caroline ;
Fagegaltier, Delphine ;
Pidoux, Josette ;
Tricoire, Herve ;
Tora, Laszlo ;
Boros, Imre M. ;
Antoniewski, Christophe .
EMBO REPORTS, 2008, 9 (02) :187-192
[10]   A critical epitope for substrate recognition by the nucleosome remodeling ATPase ISWI [J].
Clapier, CR ;
Nightingale, KP ;
Becker, PB .
NUCLEIC ACIDS RESEARCH, 2002, 30 (03) :649-655