Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions
Nucleosome–nucleosome interaction plays a fundamental role in chromatin folding and self-association. The cation-induced condensation of nucleosome core particles (NCPs) displays properties similar to those of chromatin fibers, with important contributions from the N-terminal histone tails. We study...
| Main Authors: | , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
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2012
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| Online Access: | https://hdl.handle.net/10356/79605 http://hdl.handle.net/10220/8142 |
| _version_ | 1826117167306768384 |
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| author | Liu, Ying Lu, Chenning Yang, Ye Fan, Yanping Yang, Renliang Liu, Chuan Fa Korolev, Nikolay Nordenskiöld, Lars |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Liu, Ying Lu, Chenning Yang, Ye Fan, Yanping Yang, Renliang Liu, Chuan Fa Korolev, Nikolay Nordenskiöld, Lars |
| author_sort | Liu, Ying |
| collection | NTU |
| description | Nucleosome–nucleosome interaction plays a fundamental role in chromatin folding and self-association. The cation-induced condensation of nucleosome core particles (NCPs) displays properties similar to those of chromatin fibers, with important contributions from the N-terminal histone tails. We study the self-association induced by addition of cations [Mg2+, Ca2+, cobalt(III)hexammine3+, spermidine3+ and spermine4+] for NCPs reconstituted with wild-type unmodified histones and with globular tailless histones and for NCPs with the H4 histone tail having lysine (K) acetylations or lysine-to-glutamine mutations at positions K5, K8, K12 and K16. In addition, the histone construct with the single H4K16 acetylation was investigated. Acetylated histones were prepared by a semisynthetic native chemical ligation method. The aggregation behavior of NCPs shows a general cation-dependent behavior similar to that of the self-association of nucleosome arrays. Unlike nucleosome array self-association, NCP aggregation is sensitive to position and nature of the H4 tail modification. The tetra-acetylation in the H4 tail significantly weakens the nucleosome–nucleosome interaction, while the H4 K → Q tetra-mutation displays a more modest effect. The single H4K16 acetylation also weakens the self-association of NCPs, which reflects the specific role of H4K16 in the nucleosome–nucleosome stacking. Tailless NCPs can aggregate in the presence of oligocations, which indicates that attraction also occurs by tail-independent nucleosome–nucleosome stacking and DNA–DNA attraction in the presence of cations. The experimental data were compared with the results of coarse-grained computer modeling for NCP solutions with explicit presence of mobile ions. |
| first_indexed | 2024-10-01T04:23:14Z |
| format | Journal Article |
| id | ntu-10356/79605 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:23:14Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | ntu-10356/796052023-02-28T16:56:30Z Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions Liu, Ying Lu, Chenning Yang, Ye Fan, Yanping Yang, Renliang Liu, Chuan Fa Korolev, Nikolay Nordenskiöld, Lars School of Biological Sciences DRNTU::Science::Biological sciences Nucleosome–nucleosome interaction plays a fundamental role in chromatin folding and self-association. The cation-induced condensation of nucleosome core particles (NCPs) displays properties similar to those of chromatin fibers, with important contributions from the N-terminal histone tails. We study the self-association induced by addition of cations [Mg2+, Ca2+, cobalt(III)hexammine3+, spermidine3+ and spermine4+] for NCPs reconstituted with wild-type unmodified histones and with globular tailless histones and for NCPs with the H4 histone tail having lysine (K) acetylations or lysine-to-glutamine mutations at positions K5, K8, K12 and K16. In addition, the histone construct with the single H4K16 acetylation was investigated. Acetylated histones were prepared by a semisynthetic native chemical ligation method. The aggregation behavior of NCPs shows a general cation-dependent behavior similar to that of the self-association of nucleosome arrays. Unlike nucleosome array self-association, NCP aggregation is sensitive to position and nature of the H4 tail modification. The tetra-acetylation in the H4 tail significantly weakens the nucleosome–nucleosome interaction, while the H4 K → Q tetra-mutation displays a more modest effect. The single H4K16 acetylation also weakens the self-association of NCPs, which reflects the specific role of H4K16 in the nucleosome–nucleosome stacking. Tailless NCPs can aggregate in the presence of oligocations, which indicates that attraction also occurs by tail-independent nucleosome–nucleosome stacking and DNA–DNA attraction in the presence of cations. The experimental data were compared with the results of coarse-grained computer modeling for NCP solutions with explicit presence of mobile ions. 2012-05-24T00:46:13Z 2019-12-06T13:29:08Z 2012-05-24T00:46:13Z 2019-12-06T13:29:08Z 2011 2011 Journal Article Liu, Y., Lu, C., Yang, Y., Fan, Y., Yang, R., Liu, C. F., et al. (2011). Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions. Journal of molecular biology, 414(5), 749–764. https://hdl.handle.net/10356/79605 http://hdl.handle.net/10220/8142 10.1016/j.jmb.2011.10.031 165585 en Journal of molecular biology © 2011 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of molecular biology, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [DOI: http://dx.doi.org/10.1016/j.jmb.2011.10.031 ] 45 p. application/pdf |
| spellingShingle | DRNTU::Science::Biological sciences Liu, Ying Lu, Chenning Yang, Ye Fan, Yanping Yang, Renliang Liu, Chuan Fa Korolev, Nikolay Nordenskiöld, Lars Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title | Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title_full | Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title_fullStr | Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title_full_unstemmed | Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title_short | Influence of histone tails and H4 tail acetylations on nucleosome–nucleosome interactions |
| title_sort | influence of histone tails and h4 tail acetylations on nucleosome nucleosome interactions |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/79605 http://hdl.handle.net/10220/8142 |
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