The dissociation of nuclear proteins from superhelical DNA.
Structures retaining many of the morphological features of nuclei may be released by gently lysing human cells in solutions containing non-ionic detergents and high concentrations of salt. These nucleoids contain superhelical DNA. Using a double-labelling procedure we have compared, at different sal...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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1978
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| _version_ | 1797098723084337152 |
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| author | Levin, J Jost, E Cook, P |
| author_facet | Levin, J Jost, E Cook, P |
| author_sort | Levin, J |
| collection | OXFORD |
| description | Structures retaining many of the morphological features of nuclei may be released by gently lysing human cells in solutions containing non-ionic detergents and high concentrations of salt. These nucleoids contain superhelical DNA. Using a double-labelling procedure we have compared, at different salt concentrations, the amounts and types of protein associated with human nucleoides containings superhelical or relaxed DNA. We find that the slightly lysine-rich histones (H2A and H2B) but not the arginine-rich histones (H3 and H4) dissociate more slowly from nucleoids containing superhelical DNA than from those containing relaxed DNA. A protein of apparent molecular weight of 22000 also binds more tightly to superhelical DNA. We conclude that this protein and the slightly lysine-rich histones transmute free energy of supercoiling into binding energy when they bind to superhelical DNA. |
| first_indexed | 2024-03-07T05:13:42Z |
| format | Journal article |
| id | oxford-uuid:dc6c45ea-f13a-4f34-9cce-d5a1bd5bd74f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:13:42Z |
| publishDate | 1978 |
| record_format | dspace |
| spelling | oxford-uuid:dc6c45ea-f13a-4f34-9cce-d5a1bd5bd74f2022-03-27T09:17:42ZThe dissociation of nuclear proteins from superhelical DNA.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:dc6c45ea-f13a-4f34-9cce-d5a1bd5bd74fEnglishSymplectic Elements at Oxford1978Levin, JJost, ECook, PStructures retaining many of the morphological features of nuclei may be released by gently lysing human cells in solutions containing non-ionic detergents and high concentrations of salt. These nucleoids contain superhelical DNA. Using a double-labelling procedure we have compared, at different salt concentrations, the amounts and types of protein associated with human nucleoides containings superhelical or relaxed DNA. We find that the slightly lysine-rich histones (H2A and H2B) but not the arginine-rich histones (H3 and H4) dissociate more slowly from nucleoids containing superhelical DNA than from those containing relaxed DNA. A protein of apparent molecular weight of 22000 also binds more tightly to superhelical DNA. We conclude that this protein and the slightly lysine-rich histones transmute free energy of supercoiling into binding energy when they bind to superhelical DNA. |
| spellingShingle | Levin, J Jost, E Cook, P The dissociation of nuclear proteins from superhelical DNA. |
| title | The dissociation of nuclear proteins from superhelical DNA. |
| title_full | The dissociation of nuclear proteins from superhelical DNA. |
| title_fullStr | The dissociation of nuclear proteins from superhelical DNA. |
| title_full_unstemmed | The dissociation of nuclear proteins from superhelical DNA. |
| title_short | The dissociation of nuclear proteins from superhelical DNA. |
| title_sort | dissociation of nuclear proteins from superhelical dna |
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