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© Research
Publication : Proceedings of the National Academy of Sciences of the United States of America

Nicking-closing enzyme assembles nucleosome-like structures in vitro

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 01 Aug 1979

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

Link to Pubmed [PMID] – 226980

Proc. Natl. Acad. Sci. U.S.A. 1979 Aug;76(8):3779-83

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.

http://www.ncbi.nlm.nih.gov/pubmed/226980