Home LiteratureArticle Details
PMID: 8233821 Published · ppublish English Journal Article

Nucleosomal structure at hyperacetylated loci probed in nuclei by DNA-histone crosslinking.

Nucleic acids research ·Vol. 21 ·No. 20 ·1993-10-11 ·Pages 4734-8

Ebralidse KK, Hebbes TR, Clayton AL, Thorne AW, Crane-Robinson C

Abstract

Chemically induced histone-DNA crosslinking in nuclei is used to monitor structural changes in chromosomal domains containing hyperacetylated histones. Core particles harbouring the crosslinks are immunofractionated with antibodies specific for acetylated histones. Crosslinking is revealed by gel separation of tryptic peptides from core histones that carry 32P-labelled residual nucleotide. The large number of DNA-histone crosslinks retained indicates that acetylated core histone tails are not totally displaced from the DNA. Changes in the patterns of crosslinked peptides imply a restructuring of hyperacetylated histone-DNA interactions at several points within the nucleosome. This demonstrates that a distinct conformational state is adopted in acetylated nucleosomes, known to be concentrated at transcriptionally active loci.

MeSH Terms
Acetylation Animals Cell Nucleus/chemistry Chick Embryo DNA/chemistry,metabolism Histones/chemistry,metabolism Nucleosomes/chemistry Precipitin Tests
Chemicals
Histones Nucleosomes DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ebralidse K K
Biophysics Laboratories, University of Portsmouth, UK.
Hebbes T R
Clayton A L
Thorne A W
Crane-Robinson C
References (21)
21 references, click to expand
  1. The selective extraction of histone fractions from deoxyribonucleoprotein.
    Eur J Biochem. 1973 Jun 15;35(3):546-53 PMID: 4738395
  2. A positive role for histone acetylation in transcription factor access to nucleosomal DNA.
    Cell. 1993 Jan 15;72(1):73-84 PMID: 8422685
  3. Low angle x-ray diffraction studies of chromatin structure in vivo and in isolated nuclei and metaphase chromosomes.
    J Cell Biol. 1983 Apr;96(4):1120-31 PMID: 6682117
  4. One-domain interaction of histone H4 with nucleosomal core DNA is restricted to a narrow DNA segment.
    FEBS Lett. 1986 Jan 1;194(1):69-72 PMID: 3940891
  5. Histones and their modifications.
    CRC Crit Rev Biochem. 1986;20(2):201-63 PMID: 3519076
  6. A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA.
    Nature. 1988 Jan 28;331(6154):365-7 PMID: 3340182
  7. A direct link between core histone acetylation and transcriptionally active chromatin.
    EMBO J. 1988 May;7(5):1395-402 PMID: 3409869
  8. Histone acetylation reduces nucleosome core particle linking number change.
    Cell. 1989 May 5;57(3):449-57 PMID: 2541913
  9. Change in the pattern of histone binding to DNA upon transcriptional activation.
    Cell. 1989 Jul 14;58(1):27-36 PMID: 2502314
  10. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation.
    Science. 1990 Feb 16;247(4944):841-5 PMID: 2106160
  11. Histone hyperacetylation can induce unfolding of the nucleosome core particle.
    Nucleic Acids Res. 1990 May 11;18(9):2739-47 PMID: 2339060
  12. Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae.
    Proc Natl Acad Sci U S A. 1990 Aug;87(16):6286-90 PMID: 2201024
  13. Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML.
    Mol Cell Biol. 1990 Sep;10(9):4932-4 PMID: 2117703
  14. Nucleosome linking number change controlled by acetylation of histones H3 and H4.
    J Biol Chem. 1990 Nov 15;265(32):19848-52 PMID: 2123193
  15. Irresistible force meets immovable object: transcription and the nucleosome.
    Cell. 1991 Nov 29;67(5):833-6 PMID: 1959130
  16. [Structure of nucleosomes. Localization of the H2A and H2B histone segments interacting with DNA using DNA-protein crosslinking].
    Mol Biol (Mosk). 1991 Sep-Oct;25(5):1400-11 PMID: 1753964
  17. Histone acetylation and control of gene expression.
    J Cell Sci. 1991 May;99 ( Pt 1):13-20 PMID: 1757496
  18. Chromatin as an essential part of the transcriptional mechanism.
    Nature. 1992 Jan 16;355(6357):219-24 PMID: 1731219
  19. What happens to nucleosomes during transcription?
    J Biol Chem. 1992 Feb 15;267(5):2837-40 PMID: 1310672
  20. Histone acetylation and globin gene switching.
    Nucleic Acids Res. 1992 Mar 11;20(5):1017-22 PMID: 1549462
  21. Points of contact between histone H1 and the histone octamer.
    Proc Natl Acad Sci U S A. 1980 Jan;77(1):127-31 PMID: 6928607
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1993-10-11
Pages
4734-8
Language
English
Region
England
NLM ID
0411011
PMCID
PMC331498
Subset
IM
Grants
Wellcome Trust · United Kingdom
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: [email protected]