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PMID: 15632079 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates.

Molecular and cellular biology ·Vol. 25 ·No. 2 ·2005-01-00 ·Pages 797-807

Gamble MJ, Erdjument-Bromage H, Tempst P, Freedman LP, Fisher RP

Abstract

To uncover factors required for transcription by RNA polymerase II on chromatin, we fractionated a mammalian cell nuclear extract. We identified the histone chaperone TAF-I (also known as INHAT [inhibitor of histone acetyltransferase]), which was previously proposed to repress transcription, as a potent activator of chromatin transcription responsive to the vitamin D3 receptor or to Gal4-VP16. TAF-I associates with chromatin in vitro and can substitute for the related protein NAP-1 in assembling chromatin onto cloned DNA templates in cooperation with the remodeling enzyme ATP-dependent chromatin assembly factor (ACF). The chromatin assembly and transcriptional activation functions are distinct, however, and can be dissociated temporally. Efficient transcription of chromatin assembled with TAF-I still requires the presence of TAF-I during the polymerization reaction. Conversely, TAF-I cannot stimulate transcript elongation when added after the other factors necessary for assembly of a preinitiation complex on naked DNA. Thus, TAF-I is required to facilitate transcription at a step after chromatin assembly but before transcript elongation.

MeSH Terms
Cell Fractionation Chromatin/genetics,metabolism Chromosomal Proteins, Non-Histone/genetics,metabolism DNA-Binding Proteins Gene Expression Regulation Genes, Reporter HeLa Cells Histone Chaperones Humans Molecular Chaperones/genetics,metabolism RNA Polymerase II/metabolism Receptors, Calcitriol/metabolism Recombinant Fusion Proteins/genetics,metabolism Templates, Genetic Trans-Activators/metabolism Transcription Factors/genetics,metabolism Transcription, Genetic
Chemicals
Chromatin Chromosomal Proteins, Non-Histone DNA-Binding Proteins Gal-VP16 Histone Chaperones Molecular Chaperones Receptors, Calcitriol Recombinant Fusion Proteins SET protein, human Trans-Activators Transcription Factors RNA Polymerase II
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Gamble Matthew J
Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY 10021, USA.
Erdjument-Bromage Hediye
Tempst Paul
Freedman Leonard P
Fisher Robert P
References (45)
45 references, click to expand
  1. Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos.
    Mol Cell Biol. 1992 May;12(5):2241-9 PMID: 1569951
  2. Sperm chromatin decondensation by template activating factor I through direct interaction with basic proteins.
    Mol Cell Biol. 1999 Oct;19(10):6940-52 PMID: 10490631
  3. 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. 1992 Aug;12(8):3346-55 PMID: 1630450
  4. Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication.
    J Biol Chem. 1993 May 15;268(14):10582-7 PMID: 8486711
  5. Purification and partial amino acid sequence of fuctinin, an endogenous inhibitor of fucosyltransferase activities.
    Eur J Biochem. 1994 Aug 15;224(1):47-55 PMID: 8076650
  6. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney.
    Biochemistry. 1995 Feb 14;34(6):1988-96 PMID: 7531497
  7. Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis.
    Proc Natl Acad Sci U S A. 1995 May 9;92(10):4279-83 PMID: 7753797
  8. Stimulation of transcription factor binding and histone displacement by nucleosome assembly protein 1 and nucleoplasmin requires disruption of the histone octamer.
    Mol Cell Biol. 1995 Nov;15(11):6178-87 PMID: 7565770
  9. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A.
    J Biol Chem. 1996 May 10;271(19):11059-62 PMID: 8626647
  10. Evidence that Spt6p controls chromatin structure by a direct interaction with histones.
    Science. 1996 Jun 7;272(5267):1473-6 PMID: 8633238
  11. 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. 1997 Apr;17(4):1923-37 PMID: 9121440
  12. Examination of micro-tip reversed-phase liquid chromatographic extraction of peptide pools for mass spectrometric analysis.
    J Chromatogr A. 1998 Nov 27;826(2):167-81 PMID: 9871337
  13. Activation of transcription in vitro by the BRCA1 carboxyl-terminal domain.
    J Biol Chem. 1999 Jan 22;274(4):2113-7 PMID: 9890972
  14. The protein SET regulates the inhibitory effect of p21(Cip1) on cyclin E-cyclin-dependent kinase 2 activity.
    J Biol Chem. 1999 Nov 12;274(46):33161-5 PMID: 10551888
  15. Histone- and chromatin-binding activity of template activating factor-I.
    FEBS Lett. 1999 Dec 17;463(3):285-8 PMID: 10606739
  16. Purification and characterization of a human factor that assembles and remodels chromatin.
    J Biol Chem. 2000 May 19;275(20):14787-90 PMID: 10747848
  17. p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone.
    Genes Dev. 2000 Aug 1;14(15):1899-907 PMID: 10921904
  18. Orchestrated response: a symphony of transcription factors for gene control.
    Genes Dev. 2000 Oct 15;14(20):2551-69 PMID: 11040209
  19. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein.
    Cell. 2001 Jan 12;104(1):119-30 PMID: 11163245
  20. Translating the histone code.
    Science. 2001 Aug 10;293(5532):1074-80 PMID: 11498575
  21. Biochemical analysis of chromatin containing recombinant Drosophila core histones.
    J Biol Chem. 2002 Mar 8;277(10):8749-54 PMID: 11773058
  22. Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo.
    Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3517-22 PMID: 11904415
  23. Chromatin and transcription: where do we go from here.
    Curr Opin Genet Dev. 2002 Apr;12(2):249-51 PMID: 11915846
  24. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription.
    Mol Cell. 2002 Mar;9(3):541-52 PMID: 11931762
  25. A novel estrogen receptor alpha-associated protein, template-activating factor Ibeta, inhibits acetylation and transactivation.
    Mol Endocrinol. 2003 Jan;17(1):67-78 PMID: 12511607
  26. The SET protein regulates G2/M transition by modulating cyclin B-cyclin-dependent kinase 1 activity.
    J Biol Chem. 2003 Jan 10;278(2):1158-64 PMID: 12407107
  27. Histone chaperones and nucleosome assembly.
    Curr Opin Struct Biol. 2003 Feb;13(1):6-14 PMID: 12581654
  28. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor.
    Cell. 2003 Mar 7;112(5):659-72 PMID: 12628186
  29. Functional interaction of the DNA-binding transcription factor Sp1 through its DNA-binding domain with the histone chaperone TAF-I.
    J Biol Chem. 2003 Aug 1;278(31):28758-64 PMID: 12759364
  30. Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster.
    Mol Cell Biol. 2003 Sep;23(17):6129-38 PMID: 12917335
  31. FACT facilitates transcription-dependent nucleosome alteration.
    Science. 2003 Aug 22;301(5636):1090-3 PMID: 12934006
  32. Transcription elongation factors repress transcription initiation from cryptic sites.
    Science. 2003 Aug 22;301(5636):1096-9 PMID: 12934008
  33. 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. 2003 Dec;23(23):8528-41 PMID: 14612398
  34. Chromatin remodeling by RNA polymerases.
    Trends Biochem Sci. 2004 Mar;29(3):127-35 PMID: 15003270
  35. Histone chaperones, a supporting role in the limelight.
    Biochim Biophys Acta. 2004 Mar 15;1677(1-3):3-11 PMID: 15020040
  36. Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes.
    Mol Cell. 2004 Jun 4;14(5):657-66 PMID: 15175160
  37. Removal of promoter nucleosomes by disassembly rather than sliding in vivo.
    Mol Cell. 2004 Jun 4;14(5):667-73 PMID: 15175161
  38. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei.
    Nucleic Acids Res. 1983 Mar 11;11(5):1475-89 PMID: 6828386
  39. Chromatin assembly in Xenopus oocytes: in vitro studies.
    Cell. 1984 May;37(1):33-41 PMID: 6327057
  40. Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.
    Nature. 1999 Apr 29;398(6730):824-8 PMID: 10235266
  41. Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor.
    Biochem Biophys Res Commun. 1999 Jun 7;259(2):471-5 PMID: 10362532
  42. ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly.
    Genes Dev. 1999 Jun 15;13(12):1529-39 PMID: 10385622
  43. Coiled-coil structure-mediated dimerization of template activating factor-I is critical for its chromatin remodeling activity.
    J Mol Biol. 1999 Jul 9;290(2):547-57 PMID: 10390352
  44. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins.
    Nature. 1999 Jul 15;400(6741):284-8 PMID: 10421373
  45. Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates.
    J Biol Chem. 1992 Jul 5;267(19):13647-55 PMID: 1618865
Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.25.2.797-807.2005
Published
2005-01-00
Pages
797-807
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC543418
Subset
IM
Grants
NIDDK NIH HHS · R01 DK045460 · United States
NIDDK NIH HHS · R37 DK045460 · United States
NIDDK NIH HHS · DK45460 · United States
External Links
PubMed source DOI: 10.1128/MCB.25.2.797-807.2005 PMC Full Text View journal details
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