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Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability

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DOI

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Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability. / Ferreira, Helder; Somers, Joanna; Webster, Ryan; Flaus, Andrew; Owen-Hughes, Tom.

In: Molecular and Cellular Biology, Vol. 27, No. 11, 06.2007, p. 4037-4048.

Research output: Contribution to journalArticlepeer-review

Harvard

Ferreira, H, Somers, J, Webster, R, Flaus, A & Owen-Hughes, T 2007, 'Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability', Molecular and Cellular Biology, vol. 27, no. 11, pp. 4037-4048. https://doi.org/10.1128/MCB.02229-06

APA

Ferreira, H., Somers, J., Webster, R., Flaus, A., & Owen-Hughes, T. (2007). Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability. Molecular and Cellular Biology, 27(11), 4037-4048. https://doi.org/10.1128/MCB.02229-06

Vancouver

Ferreira H, Somers J, Webster R, Flaus A, Owen-Hughes T. Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability. Molecular and Cellular Biology. 2007 Jun;27(11):4037-4048. https://doi.org/10.1128/MCB.02229-06

Author

Ferreira, Helder ; Somers, Joanna ; Webster, Ryan ; Flaus, Andrew ; Owen-Hughes, Tom. / Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability. In: Molecular and Cellular Biology. 2007 ; Vol. 27, No. 11. pp. 4037-4048.

Bibtex - Download

@article{b9c046843328477e8978fec0e22e85a8,
title = "Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability",
abstract = "Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alpha N helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.",
keywords = "BASE-PAIR RESOLUTION, SACCHAROMYCES-CEREVISIAE, CORE PARTICLE, LINKER DNA, POSTTRANSLATIONAL MODIFICATIONS, LYSINE-56 ACETYLATION, ANGSTROM RESOLUTION, TERMINAL TAILS, CHROMATIN, TRANSCRIPTION",
author = "Helder Ferreira and Joanna Somers and Ryan Webster and Andrew Flaus and Tom Owen-Hughes",
year = "2007",
month = jun,
doi = "10.1128/MCB.02229-06",
language = "English",
volume = "27",
pages = "4037--4048",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "AMER SOC MICROBIOLOGY",
number = "11",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Histone tails and the H3 alpha N helix regulate nucleosome mobility and stability

AU - Ferreira, Helder

AU - Somers, Joanna

AU - Webster, Ryan

AU - Flaus, Andrew

AU - Owen-Hughes, Tom

PY - 2007/6

Y1 - 2007/6

N2 - Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alpha N helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.

AB - Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alpha N helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.

KW - BASE-PAIR RESOLUTION

KW - SACCHAROMYCES-CEREVISIAE

KW - CORE PARTICLE

KW - LINKER DNA

KW - POSTTRANSLATIONAL MODIFICATIONS

KW - LYSINE-56 ACETYLATION

KW - ANGSTROM RESOLUTION

KW - TERMINAL TAILS

KW - CHROMATIN

KW - TRANSCRIPTION

U2 - 10.1128/MCB.02229-06

DO - 10.1128/MCB.02229-06

M3 - Article

VL - 27

SP - 4037

EP - 4048

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 11

ER -

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