A carregar...
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...
Na minha lista:
| Main Authors: | , |
|---|---|
| Formato: | Artigo |
| Idioma: | en |
| Publicado em: |
1978
|
| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC392829/ https://ncbi.nlm.nih.gov/pubmed/278974 |
| Tags: |
Adicionar Tag
Sem tags, seja o primeiro a adicionar uma tag!
|
| id |
pubmed-392829 |
|---|---|
| record_format |
dspace |
| 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 |
| _version_ |
1759804341038874624 |