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Sequence-dependent histone variant positioning signatures
BACKGROUND: Nucleosome, the fundamental unit of chromatin, is formed by wrapping nearly 147bp of DNA around an octamer of histone proteins. This histone core has many variants that are different from each other by their biochemical compositions as well as biological functions. Although the depositio...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3005914/ https://www.ncbi.nlm.nih.gov/pubmed/21143812 http://dx.doi.org/10.1186/1471-2164-11-S4-S3 |
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author | Le, Ngoc Tu Ho, Tu Bao Ho, Bich Hai |
author_facet | Le, Ngoc Tu Ho, Tu Bao Ho, Bich Hai |
author_sort | Le, Ngoc Tu |
collection | PubMed |
description | BACKGROUND: Nucleosome, the fundamental unit of chromatin, is formed by wrapping nearly 147bp of DNA around an octamer of histone proteins. This histone core has many variants that are different from each other by their biochemical compositions as well as biological functions. Although the deposition of histone variants onto chromatin has been implicated in many important biological processes, such as transcription and replication, the mechanisms of how they are deposited on target sites are still obscure. RESULTS: By analyzing genomic sequences of nucleosomes bearing different histone variants from human, including H2A.Z, H3.3 and both (H3.3/H2A.Z, so-called double variant histones), we found that genomic sequence contributes in part to determining target sites for different histone variants. Moreover, dinucleotides CA/TG are remarkably important in distinguishing target sites of H2A.Z-only nucleosomes with those of H3.3-containing (both H3.3-only and double variant) nucleosomes. CONCLUSIONS: There exists a DNA-related mechanism regulating the deposition of different histone variants onto chromatin and biological outcomes thereof. This provides additional insights into epigenetic regulatory mechanisms of many important cellular processes. |
format | Text |
id | pubmed-3005914 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-30059142010-12-22 Sequence-dependent histone variant positioning signatures Le, Ngoc Tu Ho, Tu Bao Ho, Bich Hai BMC Genomics Proceedings BACKGROUND: Nucleosome, the fundamental unit of chromatin, is formed by wrapping nearly 147bp of DNA around an octamer of histone proteins. This histone core has many variants that are different from each other by their biochemical compositions as well as biological functions. Although the deposition of histone variants onto chromatin has been implicated in many important biological processes, such as transcription and replication, the mechanisms of how they are deposited on target sites are still obscure. RESULTS: By analyzing genomic sequences of nucleosomes bearing different histone variants from human, including H2A.Z, H3.3 and both (H3.3/H2A.Z, so-called double variant histones), we found that genomic sequence contributes in part to determining target sites for different histone variants. Moreover, dinucleotides CA/TG are remarkably important in distinguishing target sites of H2A.Z-only nucleosomes with those of H3.3-containing (both H3.3-only and double variant) nucleosomes. CONCLUSIONS: There exists a DNA-related mechanism regulating the deposition of different histone variants onto chromatin and biological outcomes thereof. This provides additional insights into epigenetic regulatory mechanisms of many important cellular processes. BioMed Central 2010-12-02 /pmc/articles/PMC3005914/ /pubmed/21143812 http://dx.doi.org/10.1186/1471-2164-11-S4-S3 Text en Copyright ©2010 Le et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Proceedings Le, Ngoc Tu Ho, Tu Bao Ho, Bich Hai Sequence-dependent histone variant positioning signatures |
title | Sequence-dependent histone variant positioning signatures |
title_full | Sequence-dependent histone variant positioning signatures |
title_fullStr | Sequence-dependent histone variant positioning signatures |
title_full_unstemmed | Sequence-dependent histone variant positioning signatures |
title_short | Sequence-dependent histone variant positioning signatures |
title_sort | sequence-dependent histone variant positioning signatures |
topic | Proceedings |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3005914/ https://www.ncbi.nlm.nih.gov/pubmed/21143812 http://dx.doi.org/10.1186/1471-2164-11-S4-S3 |
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