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PMID: 278974 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Compact oligomers and nucleosome phasing.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 8 ·1978-08-00 ·Pages 3583-7

Tatchell K, Van Holde KE

Abstract

Micrococcal nuclease (EC 3.1.4.7) digestion of histone H1- and H5-depleted chicken erythrocyte chromatin yields, in addition to 140-base-pair (bp) core particles, a series of nucleosome oligomers containing about 260 bp (compact dimer), 380 bp (compact trimer), etc. of DNA. These are postulated to represent members of a class of oligomers in which the DNA is tightly wound on stacked protein cores. The physical properties (melting, circular dichroism) as well as DNase I (EC 3.1.4.5) digestion patterns support this view. DNase I digestion of tight oligomers in which the 5' ends of the DNA have been labeled yields results consistent with this model and inconsistent with some other possible models. Several classes of such particles are postulated to exist, differing in DNA length by 10-bp increments. This may be an explanation of the 10-bp nucleosome "phasing" that has been observed in some nuclei.

MeSH Terms
Chromatin Circular Dichroism DNA Deoxyribonucleases Electrophoresis, Polyacrylamide Gel Models, Biological
Chemicals
Chromatin DNA Deoxyribonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Tatchell K
Van Holde K E
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23 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.75.8.3583
Published
1978-08-00
Pages
3583-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392829
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.8.3583 PMC Full Text View journal details
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