Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation (original) (raw)

• Iizuka, M. & Smith, M. M. Functional consequences of histone modifications. Curr. Opin. Genet. Dev. 13, 154–160 (2003)
  Article CAS Google Scholar
• Bottomley, M. J. Structures of protein domains that create or recognize histone modifications. EMBO Rep. 5, 464–469 (2004)
  Article CAS Google Scholar
• Torok, M. S. & Grant, P. A. Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels. Adv. Protein Chem. 67, 181–199 (2004)
  Article CAS Google Scholar
• Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41–45 (2000)
  Article ADS CAS Google Scholar
• Sims, R. J., Nishioka, K. & Reinberg, D. Histone lysine methylation: a signature for chromatin function. Trends Genet. 19, 629–639 (2003)
  Article CAS Google Scholar
• Pray-Grant, M. G. et al. The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway. Mol. Cell. Biol. 22, 8774–8786 (2002)
  Article CAS Google Scholar
• Grant, P. A. et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11, 1640–1650 (1997)
  Article CAS Google Scholar
• Sterner, D. E., Belotserkovskaya, R. & Berger, S. L. SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription. Proc. Natl Acad. Sci. USA 99, 11622–11627 (2002)
  Article ADS CAS Google Scholar
• Lee, T. I. et al. Redundant roles for the TFIID and SAGA complexes in global transcription. Nature 405, 701–704 (2000)
  Article ADS CAS Google Scholar
• Huisinga, K. L. & Pugh, B. F. A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae. Mol. Cell 13, 573–585 (2004)
  Article CAS Google Scholar
• Daniel, J. A. et al. Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription. J. Biol. Chem. 279, 1867–1871 (2004)
  Article CAS Google Scholar
• Henry, K. W. et al. Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17, 2648–2663 (2003)
  Article CAS Google Scholar
• Woodage, T., Basrai, M. A., Baxevanis, A. D., Hieter, P. & Collins, F. S. Characterization of the CHD family of proteins. Proc. Natl Acad. Sci. USA 94, 11472–11477 (1997)
  Article ADS CAS Google Scholar
• Tran, H. G., Steger, D. J., Iyer, V. R. & Johnson, A. D. The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor. EMBO J. 19, 2323–2331 (2000)
  Article CAS Google Scholar
• Krogan, N. J. et al. RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol. Cell. Biol. 22, 6979–6992 (2002)
  Article CAS Google Scholar
• Simic, R. et al. Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes. EMBO J. 22, 1846–1856 (2003)
  Article CAS Google Scholar
• Brehm, A., Tufteland, K. R., Aasland, R. & Becker, P. B. The many colours of chromodomains. Bioessays 26, 133–140 (2004)
  Article CAS Google Scholar
• Fischle, W. et al. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 17, 1870–1881 (2003)
  Article CAS Google Scholar
• Min, J., Zhang, Y. & Xu, R. M. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17, 1823–1828 (2003)
  Article CAS Google Scholar
• Stokes, D. G., Tartof, K. D. & Perry, R. P. CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes. Proc. Natl Acad. Sci. USA 93, 7137–7142 (1996)
  Article ADS CAS Google Scholar
• Kelley, D. E., Stokes, D. G. & Perry, R. P. CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin. Chromosoma 108, 10–25 (1999)
  Article CAS Google Scholar
• Bernstein, B. E. et al. Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl Acad. Sci. USA 99, 8695–8700 (2002)
  Article ADS CAS Google Scholar
• Santos-Rosa, H. et al. Active genes are tri-methylated at K4 of histone H3. Nature 419, 407–411 (2002)
  Article ADS CAS Google Scholar
• Schubeler, D. et al. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev. 18, 1263–1271 (2004)
  Article Google Scholar
• Jacobs, S. A. et al. Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3. EMBO J. 20, 5232–5241 (2001)
  Article CAS Google Scholar
• Nielsen, P. R. et al. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416, 103–107 (2002)
  Article ADS CAS Google Scholar
• Jacobs, S. A. & Khorasanizadeh, S. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295, 2080–2083 (2002)
  Article ADS CAS Google Scholar
• Krebs, J. E., Fry, C. J., Samuels, M. L. & Peterson, C. L. Global role for chromatin remodeling enzymes in mitotic gene expression. Cell 102, 587–598 (2000)
  Article CAS Google Scholar
• Santos-Rosa, H. et al. Methylation of histone H3 K4 mediates association of the Isw1p ATPase with chromatin. Mol. Cell 12, 1325–1332 (2003)
  Article CAS 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 Google Scholar