The Histone Chaperone TAF-I/SET/INHAT Is Required for Transcription In Vitro of Chromatin Templates

REFERENCES

• Adkins, M. W., S. R. Howar, and J. K. Tyler. 2004. Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes. Mol. Cell 14:657–666.
   PubMed Web of Science ®Google Scholar
• Akey, C. W., and K. Luger. 2003. Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13:6–14.
   PubMed Web of Science ®Google Scholar
• Becker, P. B., and C. Wu. 1992. Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos. Mol. Cell. Biol. 12:2241–2249.
   PubMedGoogle Scholar
• Belotserkovskaya, R., S. Oh, V. A. Bondarenko, G. Orphanides, V. M. Studitsky, and D. Reinberg. 2003. FACT facilitates transcription-dependent nucleosome alteration. Science 301:1090–1093.
   PubMed Web of Science ®Google Scholar
• Boeger, H., J. Griesenbeck, J. S. Strattan, and R. D. Kornberg. 2004. Removal of promoter nucleosomes by disassembly rather than sliding in vivo. Mol. Cell 14:667–673.
   PubMedGoogle Scholar
• Bortvin, A., and F. Winston. 1996. Evidence that Spt6p controls chromatin structure by a direct interaction with histones. Science 272:1473–1476.
   PubMed Web of Science ®Google Scholar
• Canela, N., A. Rodriguez-Vilarrupla, J. M. Estanyol, C. Diaz, M. J. Pujol, N. Agell, and O. Bachs. 2003. The SET protein regulates G2/M transition by modulating cyclin B-cyclin-dependent kinase 1 activity. J. Biol. Chem. 278:1158–1164.
   PubMed Web of Science ®Google Scholar
• Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475–1489.
   PubMed Web of Science ®Google Scholar
• Erdjument-Bromage, H., M. Lui, L. Lacomis, A. Grewal, R. S. Annan, D. E. McNulty, S. A. Carr, and P. Tempst. 1998. Examination of micro-tip reversed-phase liquid chromatographic extraction of peptide pools for mass spectrometric analysis. J. Chromatogr. A 826:167–181.
   PubMedGoogle Scholar
• Estanyol, J. M., M. Jaumot, O. Casanovas, A. Rodriguez-Vilarrupla, N. Agell, and O. Bachs. 1999. The protein SET regulates the inhibitory effect of p21(Cip1) on cyclin E-cyclin-dependent kinase 2 activity. J. Biol. Chem. 274:33161–33165.
   PubMed Web of Science ®Google Scholar
• Fan, Z., P. J. Beresford, D. Y. Oh, D. Zhang, and J. Lieberman. 2003. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell 112:659–672.
   PubMed Web of Science ®Google Scholar
• Glikin, G. C., I. Ruberti, and A. Worcel. 1984. Chromatin assembly in Xenopus oocytes: in vitro studies. Cell 37:33–41.
   PubMed Web of Science ®Google Scholar
• Haile, D. T., and J. D. Parvin. 1999. Activation of transcription in vitro by the BRCA1 carboxyl-terminal domain. J. Biol. Chem. 274:2113–2117.
   PubMed Web of Science ®Google Scholar
• Ito, T., T. Ikehara, T. Nakagawa, W. L. Kraus, and M. Muramatsu. 2000. p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone. Genes Dev. 14:1899–1907.
   PubMedGoogle Scholar
• Ito, T., M. E. Levenstein, D. V. Fyodorov, A. K. Kutach, R. Kobayashi, and J. T. Kadonaga. 1999. ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly. Genes Dev. 13:1529–1539.
   PubMed Web of Science ®Google Scholar
• Izban, M. G., and D. S. Luse. 1992. Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates. J. Biol. Chem. 267:13647–13655.
   PubMed Web of Science ®Google Scholar
• Jenuwein, T., and C. D. Allis. 2001. Translating the histone code. Science 293:1074–1080.
   PubMed Web of Science ®Google Scholar
• Kaplan, C. D., L. Laprade, and F. Winston. 2003. Transcription elongation factors repress transcription initiation from cryptic sites. Science 301:1096–1099.
   PubMed Web of Science ®Google Scholar
• Kireeva, M. L., W. Walter, V. Tchernajenko, V. Bondarenko, M. Kashlev, and V. M. Studitsky. 2002. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Mol. Cell 9:541–552.
   PubMed Web of Science ®Google Scholar
• Kornberg, R. D., and Y. Lorch. 2002. Chromatin and transcription: where do we go from here. Curr. Opin. Genet. Dev. 12:249–251.
   PubMedGoogle Scholar
• Lemon, B., and R. Tjian. 2000. Orchestrated response: a symphony of transcription factors for gene control. Genes Dev. 14:2551–2569.
   PubMed Web of Science ®Google Scholar
• Lemon, B. D., J. D. Fondell, and L. P. Freedman. 1997. Retinoid X receptor:vitamin D3 receptor heterodimers promote stable preinitiation complex formation and direct 1,25-dihydroxyvitamin D3-dependent cell-free transcription. Mol. Cell. Biol. 17:1923–1937.
   PubMedGoogle Scholar
• LeRoy, G., A. Loyola, W. S. Lane, and D. Reinberg. 2000. Purification and characterization of a human factor that assembles and remodels chromatin. J. Biol. Chem. 275:14787–14790.
   PubMedGoogle Scholar
• Levenstein, M. E., and J. T. Kadonaga. 2002. Biochemical analysis of chromatin containing recombinant Drosophila core histones. J. Biol. Chem. 277:8749–8754.
   PubMedGoogle Scholar
• Li, M., H. Guo, and Z. Damuni. 1995. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry 34:1988–1996.
   PubMed Web of Science ®Google Scholar
• Li, M., A. Makkinje, and Z. Damuni. 1996. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J. Biol. Chem. 271:11059–11062.
   PubMed Web of Science ®Google Scholar
• Loven, M. A., N. Muster, J. R. Yates, and A. M. Nardulli. 2003. A novel estrogen receptor alpha-associated protein, template-activating factor Iβ, inhibits acetylation and transactivation. Mol. Endocrinol. 17:67–78.
   PubMedGoogle Scholar
• Loyola, A., and G. Almouzni. 2004. Histone chaperones, a supporting role in the limelight. Biochim. Biophys. Acta 1677:3–11.
   PubMed Web of Science ®Google Scholar
• Matsumoto, K., K. Nagata, M. Miyaji-Yamaguchi, A. Kikuchi, and M. Tsujimoto. 1999. Sperm chromatin decondensation by template activating factor I through direct interaction with basic proteins. Mol. Cell. Biol. 19:6940–6952.
   PubMedGoogle Scholar
• Matsumoto, K., K. Nagata, M. Okuwaki, and M. Tsujimoto. 1999. Histone- and chromatin-binding activity of template activating factor-I. FEBS Lett. 463:285–288.
   PubMedGoogle Scholar
• Matsumoto, K., K. Nagata, M. Ui, and F. Hanaoka. 1993. Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication. J. Biol. Chem. 268:10582–10587.
   PubMedGoogle Scholar
• Miyaji-Yamaguchi, M., M. Okuwaki, and K. Nagata. 1999. Coiled-coil structure-mediated dimerization of template activating factor-I is critical for its chromatin remodeling activity. J. Mol. Biol. 290:547–557.
   PubMed Web of Science ®Google Scholar
• Miyamoto, S., T. Suzuki, S. Muto, K. Aizawa, A. Kimura, Y. Mizuno, T. Nagino, Y. Imai, N. Adachi, M. Horikoshi, and R. Nagai. 2003. Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain. Mol. Cell. Biol. 23:8528–8541.
   PubMed Web of Science ®Google Scholar
• Nagata, K., H. Kawase, H. Handa, K. Yano, M. Yamasaki, Y. Ishimi, A. Okuda, A. Kikuchi, and K. Matsumoto. 1995. Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis. Proc. Natl. Acad. Sci. USA 92:4279–4283.
   PubMedGoogle Scholar
• Nowak, S. J., C. Y. Pai, and V. G. Corces. 2003. Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster. Mol. Cell. Biol. 23:6129–6138.
   PubMedGoogle Scholar
• Orphanides, G., W. H. Wu, W. S. Lane, M. Hampsey, and D. Reinberg. 1999. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature 400:284–288.
   PubMed Web of Science ®Google Scholar
• Rachez, C., B. D. Lemon, Z. Suldan, V. Bromleigh, M. Gamble, A. M. Naar, H. Erdjument-Bromage, P. Tempst, and L. P. Freedman. 1999. Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature 398:824–828.
   PubMed Web of Science ®Google Scholar
• Ruggiero-Lopez, D., C. Manioc, C. Geourjon, P. Louisot, and A. Martin. 1994. Purification and partial amino acid sequence of fuctinin, an endogenous inhibitor of fucosyltransferase activities. Eur. J. Biochem. 224:47–55.
   PubMedGoogle Scholar
• Saito, S., M. Miyaji-Yamaguchi, T. Shimoyama, and K. Nagata. 1999. Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor. Biochem. Biophys. Res. Commun. 259:471–475.
   PubMedGoogle Scholar
• Seo, S. B., P. McNamara, S. Heo, A. Turner, W. S. Lane, and D. Chakravarti. 2001. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell 104:119–130.
   PubMed Web of Science ®Google Scholar
• Studitsky, V. M., W. Walter, M. Kireeva, M. Kashlev, and G. Felsenfeld. 2004. Chromatin remodeling by RNA polymerases. Trends Biochem. Sci. 29:127–135.
   PubMedGoogle Scholar
• Suzuki, T., S. Muto, S. Miyamoto, K. Aizawa, M. Horikoshi, and R. Nagai. 2003. Functional interaction of the DNA-binding transcription factor Sp1 through its DNA-binding domain with the histone chaperone TAF-I. J. Biol. Chem. 278:28758–28764.
   PubMedGoogle Scholar
• von Lindern, M., S. van Baal, J. Wiegant, A. Raap, A. Hagemeijer, and G. Grosveld. 1992. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: characterization of the set gene. Mol. Cell. Biol. 12:3346–3355.
   PubMed Web of Science ®Google Scholar
• Walter, P. P., T. A. Owen-Hughes, J. Cote, and J. L. Workman. 1995. Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer. Mol. Cell. Biol. 15:6178–6187.
   PubMedGoogle Scholar
• Winkler, G. S., A. Kristjuhan, H. Erdjument-Bromage, P. Tempst, and J. Q. Svejstrup. 2002. Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proc. Natl. Acad. Sci. USA 99:3517–3522.
   PubMed Web of Science ®Google Scholar