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PMID: 226980 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Nicking-closing enzyme assembles nucleosome-like structures in vitro.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 8 ·1979-08-00 ·Pages 3779-83

Germond JE, Rouvière-Yaniv J, Yaniv M, Brutlag D

Abstract

The four core histones (H2A, H2B, H3, and H4) and DNA were assembled into nucleosome-like particles at physiological ionic strengths either by an extract of chromatin rich in nicking-closing activity or by the purified nicking-closing enzyme itself. When histone-DNA complexes were assembled in vitro from relaxed circular DNA, nearly physiological numbers of superhelical turns were induced in the DNA molecule. Electron microscopy of the complexes assembled by the chromatin extract revealed a beaded structure and a reduction of the contour length compared to free DNA. Micrococcal nuclease digestion of the histone-DNA complexes yielded 145-base-pair DNA fragments typical of nucleosome core particles and shorter subnucleosomal DNA fragments of discrete length.

MeSH Terms
Animals Bacteriocin Plasmids Chromatin/ultrastructure DNA Topoisomerases, Type I/metabolism DNA, Bacterial/metabolism DNA, Circular/metabolism DNA, Superhelical/metabolism Drosophila melanogaster Histones/metabolism Micrococcal Nuclease/metabolism Nucleosomes/metabolism,ultrastructure Rats
Chemicals
Chromatin DNA, Bacterial DNA, Circular DNA, Superhelical Histones Nucleosomes Micrococcal Nuclease DNA Topoisomerases, Type I
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Germond J E
Rouvière-Yaniv J
Yaniv M
Brutlag D
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29 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.76.8.3779
Published
1979-08-00
Pages
3779-83
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383917
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.76.8.3779 PMC Full Text View journal details
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