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

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.

authors

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

doi

10.1073/pnas.76.8.3779

subject

Has Abstract

pub_date

1979-08-01 00:00:00

pages

3779-83

issue

8

eissn

0027-8424

issn

1091-6490

journal_volume

76

pub_type

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