ATAC is a double histone acetyltransferase complex that stimulates nucleosome sliding (original) (raw)

• de la Cruz, X., Lois, S., Sanchez-Molina, S. & Martinez-Balbas, M.A. Do protein motifs read the histone code? Bioessays 27, 164–175 (2005).
  Article CAS PubMed Google Scholar
• Allis, C.D. et al. New nomenclature for chromatin-modifying enzymes. Cell 131, 633–636 (2007).
  Article CAS PubMed Google Scholar
• Eberharter, A. & Becker, P.B. ATP-dependent nucleosome remodelling: factors and functions. J. Cell Sci. 117, 3707–3711 (2004).
  Article CAS PubMed Google Scholar
• Choudhary, P. & Varga-Weisz, P. ATP-dependent chromatin remodelling: action and reaction. Subcell. Biochem. 41, 29–43 (2007).
  Article PubMed Google Scholar
• Tsukiyama, T. & Wu, C. Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell 83, 1011–1020 (1995).
  Article CAS PubMed Google Scholar
• Ito, T., Bulger, M., Pazin, M.J., Kobayashi, R. & Kadonaga, J.T. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90, 145–155 (1997).
  Article CAS PubMed Google Scholar
• Varga-Weisz, P.D. et al. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature 388, 598–602 (1997).
  Article CAS PubMed Google Scholar
• Lall, S. Primers on chromatin. Nat. Struct. Mol. Biol. 14, 1110–1115 (2007).
  Article CAS PubMed Google Scholar
• Corona, D.F. et al. Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally regulated subunits of chromatin accessibility complex (CHRAC). EMBO J. 19, 3049–3059 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Eberharter, A. et al. Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome remodelling. EMBO J. 20, 3781–3788 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Hartlepp, K.F. et al. The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. Mol. Cell. Biol. 25, 9886–9896 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Kasten, M. et al. Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14. EMBO J. 23, 1348–1359 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Dhalluin, C. et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399, 491–496 (1999).
  Article CAS PubMed Google Scholar
• Hassan, A.H., Neely, K.E. & Workman, J.L. Histone acetyltransferase complexes stabilize SWI–SNF binding to promoter nucleosomes. Cell 104, 817–827 (2001).
  Article CAS PubMed Google Scholar
• Chandy, M., Gutierrez, J.L., Prochasson, P. & Workman, J.L. SWI/SNF displaces SAGA-acetylated nucleosomes. Eukaryot. Cell 5, 1738–1747 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Carey, M., Li, B. & Workman, J.L. RSC exploits histone acetylation to abrogate the nucleosomal block to RNA polymerase II elongation. Mol. Cell 24, 481–487 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Hassan, A.H., Awad, S. & Prochasson, P. The Swi2/Snf2 bromodomain is required for the displacement of SAGA and the octamer transfer of SAGA-acetylated nucleosomes. J. Biol. Chem. 281, 18126–18134 (2006).
  Article CAS PubMed Google Scholar
• Lee, K.K. & Workman, J.L. Histone acetyltransferase complexes: one size doesn't fit all. Nat. Rev. Mol. Cell Biol. 8, 284–295 (2007).
  Article CAS PubMed Google Scholar
• Kimura, A., Matsubara, K. & Horikoshi, M. A decade of histone acetylation: marking eukaryotic chromosomes with specific codes. J. Biochem. 138, 647–662 (2005).
  Article CAS PubMed Google Scholar
• Carrozza, M.J., Utley, R.T., Workman, J.L. & Cote, J. The diverse functions of histone acetyltransferase complexes. Trends Genet. 19, 321–329 (2003).
  Article CAS PubMed Google Scholar
• Timmers, H.T. & Tora, L. SAGA unveiled. Trends Biochem. Sci. 30, 7–10 (2005).
  Article CAS PubMed Google Scholar
• Daniel, J.A. & Grant, P.A. Multi-tasking on chromatin with the SAGA coactivator complexes. Mutat. Res. 618, 135–148 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Sterner, D.E. et al. Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction. Mol. Cell. Biol. 19, 86–98 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Balasubramanian, R., Pray-Grant, M.G., Selleck, W., Grant, P.A. & Tan, S. Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. J. Biol. Chem. 277, 7989–7995 (2002).
  Article CAS PubMed Google Scholar
• Kusch, T., Guelman, S., Abmayr, S.M. & Workman, J.L. Two Drosophila Ada2 homologues function in different multiprotein complexes. Mol. Cell. Biol. 23, 3305–3319 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Muratoglu, S. et al. Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes. Mol. Cell. Biol. 23, 306–321 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Barlev, N.A. et al. A novel human Ada2 homologue functions with Gcn5 or Brg1 to coactivate transcription. Mol. Cell. Biol. 23, 6944–6957 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Guelman, S. et al. Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/dGcn5-containing histone acetyltransferase complex in Drosophila. Mol. Cell. Biol. 26, 871–882 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Goppelt, A. & Meisterernst, M. Characterization of the basal inhibitor of class II transcription NC2 from Saccharomyces cerevisiae. Nucleic Acids Res. 24, 4450–4455 (1996).
  Article CAS PubMed PubMed Central Google Scholar
• Hollmann, M., Simmerl, E., Schafer, U. & Schafer, M.A. The essential Drosophila melanogaster gene wds (will die slowly) codes for a WD-repeat protein with seven repeats. Mol. Genet. Genomics 268, 425–433 (2002).
  Article CAS PubMed Google Scholar
• Mendjan, S. et al. Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol. Cell 21, 811–823 (2006).
  Article CAS PubMed Google Scholar
• Carre, C., Szymczak, D., Pidoux, J. & Antoniewski, C. The histone H3 acetylase dGcn5 is a key player in Drosophila melanogaster metamorphosis. Mol. Cell. Biol. 25, 8228–8238 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Yokoyama, A. et al. Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol. Cell. Biol. 24, 5639–5649 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Grant, P.A., Berger, S.L. & Workman, J.L. Identification and analysis of native nucleosomal histone acetyltransferase complexes. Methods Mol. Biol. 119, 311–317 (1999).
  CAS PubMed Google Scholar
• Kuo, M.H. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269–272 (1996).
  Article CAS PubMed Google Scholar
• Ciurciu, A., Komonyi, O., Pankotai, T. & Boros, I.M. The Drosophila histone acetyltransferase Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation. Mol. Cell. Biol. 26, 9413–9423 (2006).
  Article CAS PubMed PubMed Central Google Scholar
• Hilfiker, A., Hilfiker-Kleiner, D., Pannuti, A. & Lucchesi, J.C. mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. EMBO J. 16, 2054–2060 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Kamada, K. et al. Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex. Cell 106, 71–81 (2001).
  Article CAS PubMed Google Scholar
• Aasland, R., Stewart, A.F. & Gibson, T. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 21, 87–88 (1996).
  CAS PubMed Google Scholar
• Kukimoto, I., Elderkin, S., Grimaldi, M., Oelgeschlager, T. & Varga-Weisz, P.D. The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding and assembly mediated by ACF. Mol. Cell 13, 265–277 (2004).
  Article CAS PubMed Google Scholar
• Vary, J.C., Jr et al. Yeast Isw1p forms two separable complexes in vivo. Mol. Cell. Biol. 23, 80–91 (2003).
  Article CAS PubMed Google Scholar
• Stockdale, C., Flaus, A., Ferreira, H. & Owen-Hughes, T. Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes. J. Biol. Chem. 281, 16279–16288 (2006).
  Article CAS PubMed Google Scholar
• Yang, J.G., Madrid, T.S., Sevastopoulos, E. & Narlikar, G.J. The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor that regulates nucleosome spacing. Nat. Struct. Mol. Biol. 13, 1078–1083 (2006).
  Article CAS PubMed Google Scholar
• Mohrmann, L. et al. Differential targeting of two distinct SWI/SNF-related Drosophila chromatin-remodeling complexes. Mol. Cell. Biol. 24, 3077–3088 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Katsani, K.R., Mahmoudi, T. & Verrijzer, C.P. Selective gene regulation by SWI/SNF-related chromatin remodeling factors. Curr. Top. Microbiol. Immunol. 274, 113–141 (2003).
  CAS PubMed Google Scholar
• Jacobson, R.H., Ladurner, A.G., King, D.S. & Tjian, R. Structure and function of a human TAFII250 double bromodomain module. Science 288, 1422–1425 (2000).
  Article CAS PubMed Google Scholar
• Hassan, A.H. et al. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 111, 369–379 (2002).
  Article CAS PubMed Google Scholar
• Ferreira, R. et al. Site-specific acetylation of ISWI by GCN5. BMC Mol. Biol. 8, 73 (2007).
  Article PubMed PubMed Central Google Scholar
• Rudolph, M.J., Wuebbens, M.M., Turque, O., Rajagopalan, K.V. & Schindelin, H. Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. J. Biol. Chem. 278, 14514–14522 (2003).
  Article CAS PubMed Google Scholar
• Corona, D.F., Clapier, C.R., Becker, P.B. & Tamkun, J.W. Modulation of ISWI function by site-specific histone acetylation. EMBO Rep. 3, 242–247 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Shogren-Knaak, M. et al. Histone H4–K16 acetylation controls chromatin structure and protein interactions. Science 311, 844–847 (2006).
  Article CAS PubMed Google Scholar
• Suganuma, T., Kawabata, M., Ohshima, T. & Ikeda, M.A. Growth suppression of human carcinoma cells by reintroduction of the p300 coactivator. Proc. Natl. Acad. Sci. USA 99, 13073–13078 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030–1032 (1999).
  Article CAS PubMed Google Scholar
• Lee, K.K., Florens, L., Swanson, S.K., Washburn, M.P. & Workman, J.L. The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex. Mol. Cell. Biol. 25, 1173–1182 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Eberharter, A., John, S., Grant, P.A., Utley, R.T. & Workman, J.L. Identification and analysis of yeast nucleosomal histone acetyltransferase complexes. Methods 15, 315–321 (1998).
  Article CAS PubMed Google Scholar
• Thastrom, A., Bingham, L.M. & Widom, J. Nucleosomal locations of dominant DNA sequence motifs for histone-DNA interactions and nucleosome positioning. J. Mol. Biol. 338, 695–709 (2004).
  Article CAS PubMed Google Scholar
• Gutierrez, J. et al. Interaction of CBFα/AML/PEBP2α transcription factors with nucleosomes containing promoter sequences requires flexibility in the translational positioning of the histone octamer and exposure of the CBFα site. Biochemistry 39, 13565–13574 (2000).
  Article CAS PubMed Google Scholar
• Utley, R.T. et al. In vitro analysis of transcription factor binding to nucleosomes and nucleosome disruption/displacement. Methods Enzymol. 274, 276–291 (1996).
  Article CAS PubMed Google Scholar
• Gutierrez, J.L., Chandy, M., Carrozza, M.J. & Workman, J.L. Activation domains drive nucleosome eviction by SWI/SNF. EMBO J. 26, 730–740 (2007).
  Article CAS PubMed PubMed Central Google Scholar
• Tomomori-Sato, C. et al. A mammalian mediator subunit that shares properties with Saccharomyces cerevisiae mediator subunit Cse2. J. Biol. Chem. 279, 5846–5851 (2004).
  Article CAS PubMed Google Scholar
• Keller, C.A., Grill, M.A. & Abmayr, S.M. A role for nautilus in the differentiation of muscle precursors. Dev. Biol. 202, 157–171 (1998).
  Article CAS PubMed Google Scholar