Home LiteratureArticle Details
PMID: 11571273 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Physical and functional association of SU(VAR)3-9 and HDAC1 in Drosophila.

EMBO reports ·Vol. 2 ·No. 10 ·2001-10-00 ·Pages 915-9

Czermin B, Schotta G, Hülsmann BB, Brehm A, Becker PB, Reuter G, Imhof A

Abstract

Modification of histones can have a dramatic impact on chromatin structure and function. Acetylation of lysines within the N-terminal tail of the histone octamer marks transcriptionally active regions of the genome whereas deacetylation seems to play a role in transcriptional silencing. Recently, the methylation of the histone tails has also been shown to be important for transcriptional regulation and chromosome structure. Here we show by immunoaffinity purification that two activities important for chromatin-mediated gene silencing, the histone methyltransferase SU(VAR)3-9 and the histone deacetylase HDAC1, associate in vivo. The two activities cooperate to methylate pre-acetylated histones. Both enzymes are modifiers of position effect variegation and interact genetically in flies. We suggest a model in which the concerted histone deacetylation and methylation by a SU(VAR)3-9/HDAC1-containing complex leads to a permanent silencing of transcription in particular areas of the genome.

MeSH Terms
Animals Blotting, Western Chromatin/metabolism Drosophila Fungal Proteins Gene Silencing Genes, Dominant Genome Histone Deacetylase 1 Histone Deacetylases/chemistry,metabolism Histones/metabolism Lysine/metabolism Methylation Methyltransferases/chemistry,metabolism Mutation Precipitin Tests Protein Binding Protein Structure, Tertiary Recombinant Proteins/metabolism Salts/pharmacology Transcription, Genetic
Chemicals
Chromatin Fungal Proteins Histones Recombinant Proteins Salts Methyltransferases SU(VAR)3-9 HDAC1 protein, human Histone Deacetylase 1 Histone Deacetylases Lysine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Czermin B
Adolf-Butenandt Institut, Molekularbiologie, Ludwig-Maximilians Universität, Schillerstrasse 44, D-80336 München, Germany.
Schotta G
Hülsmann B B
Brehm A
Becker P B
Reuter G
Imhof A
References (29)
29 references, click to expand
  1. Dynamic methylation of alfalfa histone H3.
    J Biol Chem. 1993 Mar 5;268(7):4918-21 PMID: 8444870
  2. Position-effect variegation after 60 years.
    Trends Genet. 1990 Dec;6(12):422-6 PMID: 2087785
  3. Position effect variegation and chromatin proteins.
    Bioessays. 1992 Sep;14(9):605-12 PMID: 1365916
  4. The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast.
    Nature. 1996 Dec 12;384(6609):589-91 PMID: 8955276
  5. Histone acetylation: chromatin in action.
    Trends Biochem Sci. 1997 Apr;22(4):128-32 PMID: 9149532
  6. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.
    Cell. 1997 May 2;89(3):357-64 PMID: 9150135
  7. Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres.
    Cell. 1997 Dec 26;91(7):1021-32 PMID: 9428524
  8. Retinoblastoma protein recruits histone deacetylase to repress transcription.
    Nature. 1998 Feb 5;391(6667):597-601 PMID: 9468139
  9. Linking histone acetylation to transcriptional regulation.
    Cell Mol Life Sci. 1998 Jan;54(1):6-20 PMID: 9487383
  10. Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription.
    Nat Genet. 1998 Jun;19(2):187-91 PMID: 9620779
  11. The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast.
    Nat Genet. 1998 Jun;19(2):192-5 PMID: 9620780
  12. A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation.
    Cell. 1998 Jul 10;94(1):45-53 PMID: 9674426
  13. The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes.
    Trends Cell Biol. 1998 May;8(5):193-7 PMID: 9695838
  14. Roles of histone acetyltransferases and deacetylases in gene regulation.
    Bioessays. 1998 Aug;20(8):615-26 PMID: 9780836
  15. Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31.
    EMBO J. 1999 Apr 1;18(7):1923-38 PMID: 10202156
  16. The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo.
    Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6797-801 PMID: 10359792
  17. Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation.
    Genes Dev. 1999 Aug 1;13(15):1924-35 PMID: 10444591
  18. Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation.
    Nat Genet. 1999 Sep;23(1):62-6 PMID: 10471500
  19. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p.
    EMBO J. 1999 Sep 15;18(18):5108-19 PMID: 10487762
  20. The language of covalent histone modifications.
    Nature. 2000 Jan 6;403(6765):41-5 PMID: 10638745
  21. Mutational analysis of a histone deacetylase in Drosophila melanogaster: missense mutations suppress gene silencing associated with position effect variegation.
    Genetics. 2000 Feb;154(2):657-68 PMID: 10655219
  22. The genome sequence of Drosophila melanogaster.
    Science. 2000 Mar 24;287(5461):2185-95 PMID: 10731132
  23. Regulation of chromatin structure by site-specific histone H3 methyltransferases.
    Nature. 2000 Aug 10;406(6796):593-9 PMID: 10949293
  24. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.
    Nature. 2001 Mar 1;410(6824):116-20 PMID: 11242053
  25. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.
    Nature. 2001 Mar 1;410(6824):120-4 PMID: 11242054
  26. Modifications of the histone N-terminal domains. Evidence for an "epigenetic code"?
    Mol Biotechnol. 2001 Jan;17(1):1-13 PMID: 11280927
  27. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly.
    Science. 2001 Apr 6;292(5514):110-3 PMID: 11283354
  28. Single-locus modification of position-effect variegation in Drosophila melanogaster. I. White variegation.
    Genetics. 1967 Dec;57(4):751-66 PMID: 6082620
  29. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes.
    EMBO J. 1994 Aug 15;13(16):3822-31 PMID: 7915232
Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-221X
Published
2001-10-00
Epub
2001-00-24
Pages
915-9
Language
English
Region
England
NLM ID
100963049
PMCID
PMC1084088
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com