Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin

Karl Nightingale, Stefan Dimitrov, Raymond Reeves, Alan P. Wolffe

Research output: Contribution to journalArticle

142 Citations (Scopus)

Abstract

The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.

Original languageEnglish
Pages (from-to)548-561
Number of pages14
JournalEMBO Journal
Volume15
Issue number3
Publication statusPublished - 1 Feb 1996
Externally publishedYes

Fingerprint

HMGB1 Protein
Histones
Chromatin
Xenopus
Nucleosomes
High Mobility Group Proteins
DNA
Digestion
Micrococcal Nuclease
Deoxyribonuclease I
Hydroxyl Radical
Ovum
Spermatozoa

Keywords

  • B4/HMG1/nucleosome/Xenopus
  • Chromatin/histone

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin. / Nightingale, Karl; Dimitrov, Stefan; Reeves, Raymond; Wolffe, Alan P.

In: EMBO Journal, Vol. 15, No. 3, 01.02.1996, p. 548-561.

Research output: Contribution to journalArticle

Nightingale, Karl ; Dimitrov, Stefan ; Reeves, Raymond ; Wolffe, Alan P. / Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin. In: EMBO Journal. 1996 ; Vol. 15, No. 3. pp. 548-561.
@article{f9bd98bf42f04dac980b2f3fa35bbfa1,
title = "Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin",
abstract = "The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.",
keywords = "B4/HMG1/nucleosome/Xenopus, Chromatin/histone",
author = "Karl Nightingale and Stefan Dimitrov and Raymond Reeves and Wolffe, {Alan P.}",
year = "1996",
month = "2",
day = "1",
language = "English",
volume = "15",
pages = "548--561",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "3",

}

TY - JOUR

T1 - Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin

AU - Nightingale, Karl

AU - Dimitrov, Stefan

AU - Reeves, Raymond

AU - Wolffe, Alan P.

PY - 1996/2/1

Y1 - 1996/2/1

N2 - The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.

AB - The high mobility group proteins 1 and 2 (HMG1/2) and histone B4 are major components of chromatin within the nuclei assembled during the incubation of Xenopus sperm chromatin in Xenopus egg extract. To investigate their potential structural and functional roles, we have cloned and expressed Xenopus HMG1 and histone B4. Purified histone B4 and HMG1 form stable complexes with nucleosomes including Xenopus 5S DNA. Both proteins associate with linker DNA and stabilize it against digestion with micrococcal nuclease, in a similar manner to histone H1. However, neither histone B4 nor HMG1 influence the DNase I or hydroxyl radical digestion of DNA within the nucleosome core. We suggest that HMG1/2 and histone B4 have a shared structural role in organizing linker DNA in the nucleosome.

KW - B4/HMG1/nucleosome/Xenopus

KW - Chromatin/histone

UR - http://www.scopus.com/inward/record.url?scp=0030064348&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030064348&partnerID=8YFLogxK

M3 - Article

C2 - 8599938

AN - SCOPUS:0030064348

VL - 15

SP - 548

EP - 561

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 3

ER -