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Compact oligomers and nucleosome phasing.

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 r...

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Main Authors: Tatchell, K, Van Holde, K E
Formato: Artigo
Idioma:en
Publicado em: 1978
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC392829/
https://ncbi.nlm.nih.gov/pubmed/278974
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spelling pubmed-3928292004-07-30 Compact oligomers and nucleosome phasing. Tatchell, K Van Holde, K E Proc Natl Acad Sci U S A Research Article 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. 1978-08 /pmc/articles/PMC392829/ /pubmed/278974 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Tatchell, K
Van Holde, K E
Compact oligomers and nucleosome phasing.
description 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.
author Tatchell, K
Van Holde, K E
author_facet Tatchell, K
Van Holde, K E
author_sort Tatchell, K
title Compact oligomers and nucleosome phasing.
title_short Compact oligomers and nucleosome phasing.
title_full Compact oligomers and nucleosome phasing.
title_fullStr Compact oligomers and nucleosome phasing.
title_full_unstemmed Compact oligomers and nucleosome phasing.
title_sort compact oligomers and nucleosome phasing.
publishDate 1978
url https://ncbi.nlm.nih.gov/pmc/articles/PMC392829/
https://ncbi.nlm.nih.gov/pubmed/278974
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