Literature DB >> 8233821

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

K K Ebralidse1, T R Hebbes, A L Clayton, A W Thorne, C Crane-Robinson.   

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.

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Year:  1993        PMID： 8233821      PMCID： PMC331498          DOI： 10.1093/nar/21.20.4734

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN： 0305-1048            Impact factor:   16.971


  21 in total

1.  Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation.

Authors:  P C Megee; B A Morgan; B A Mittman; M M Smith
Journal:  Science       Date:  1990-02-16       Impact factor: 47.728

2.  Histone acetylation reduces nucleosome core particle linking number change.

Authors:  V G Norton; B S Imai; P Yau; E M Bradbury
Journal:  Cell       Date:  1989-05-05       Impact factor: 41.582

3.  Change in the pattern of histone binding to DNA upon transcriptional activation.

Authors:  G A Nacheva; D Y Guschin; O V Preobrazhenskaya; V L Karpov; K K Ebralidse; A D Mirzabekov
Journal:  Cell       Date:  1989-07-14       Impact factor: 41.582

4.  The selective extraction of histone fractions from deoxyribonucleoprotein.

Authors:  L A Bolund; E W Johns
Journal:  Eur J Biochem       Date:  1973-06-15

Review 5.  Histones and their modifications.

Authors:  R S Wu; H T Panusz; C L Hatch; W M Bonner
Journal:  CRC Crit Rev Biochem       Date:  1986

6.  One-domain interaction of histone H4 with nucleosomal core DNA is restricted to a narrow DNA segment.

Authors:  K K Ebralidse; A D Mirzabekov
Journal:  FEBS Lett       Date:  1986-01-01       Impact factor: 4.124

7.  A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA.

Authors:  K K Ebralidse; S A Grachev; A D Mirzabekov
Journal:  Nature       Date:  1988-01-28       Impact factor: 49.962

8.  A positive role for histone acetylation in transcription factor access to nucleosomal DNA.

Authors:  D Y Lee; J J Hayes; D Pruss; A P Wolffe
Journal:  Cell       Date:  1993-01-15       Impact factor: 41.582

9.  A direct link between core histone acetylation and transcriptionally active chromatin.

Authors:  T R Hebbes; A W Thorne; C Crane-Robinson
Journal:  EMBO J       Date:  1988-05       Impact factor: 11.598

10.  Low angle x-ray diffraction studies of chromatin structure in vivo and in isolated nuclei and metaphase chromosomes.

Authors:  J P Langmore; J R Paulson
Journal:  J Cell Biol       Date:  1983-04       Impact factor: 10.539
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  3 in total

1.  Persistent interactions of core histone tails with nucleosomal DNA following acetylation and transcription factor binding.

Authors:  V Mutskov; D Gerber; D Angelov; J Ausio; J Workman; S Dimitrov
Journal:  Mol Cell Biol       Date:  1998-11       Impact factor: 4.272

Review 2.  What determines the folding of the chromatin fiber?

Authors:  K van Holde; J Zlatanova
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-01       Impact factor: 11.205

Review 3.  Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin.

Authors:  J R Davie
Journal:  Mol Biol Rep       Date:  1997-08       Impact factor: 2.316
  3 in total

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