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Compact oligomers and nucleosome phasing.

K Tatchell, K E Van Holde

Proceedings of the National Academy of Sciences of the United States of America

|August 1, 1978

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Researchers digested chromatin and found tightly wound nucleosome oligomers. These compact structures, differing by 10-base-pair increments, may explain nucleosome phasing in nuclei.

Area of Science:

Molecular Biology
Chromatin Structure

Background:

Chicken erythrocyte chromatin contains histones H1 and H5.
Nucleosomes are the basic units of DNA packaging in eukaryotes.

Purpose of the Study:

To investigate the structure of nucleosome oligomers formed after micrococcal nuclease digestion.
To explore the physical properties and DNAse I digestion patterns of these oligomers.

Main Methods:

Micrococcal nuclease digestion of histone H1- and H5-depleted chicken erythrocyte chromatin.
Analysis of DNA lengths and physical properties (melting, circular dichroism).
DNase I digestion of labeled tight oligomers.

Main Results:

Identified nucleosome oligomers with DNA lengths of approximately 260 bp (dimer) and 380 bp (trimer).

Related Experiment Videos

Observed physical properties and DNase I digestion patterns supporting a model of tightly wound DNA on stacked protein cores.

Found evidence for oligomer classes differing by 10-base-pair DNA increments.

Conclusions:

Postulated the existence of compact nucleosome oligomers with tightly wound DNA.
This model may explain the observed 10-bp nucleosome phasing in some nuclei.