Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Le, Ngoc Tu, Ho, Tu Bao, Ho, Bich Hai
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
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
_version_ 1782194145602830336
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
work_keys_str_mv AT lengoctu sequencedependenthistonevariantpositioningsignatures
AT hotubao sequencedependenthistonevariantpositioningsignatures
AT hobichhai sequencedependenthistonevariantpositioningsignatures