Histone chaperone networks shaping chromatin function

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Histone chaperone networks shaping chromatin function. / Hammond, Colin; Strømme, Caroline Bianchi; Huang, Hongda; Patel, Dinshaw J; Groth, Anja.

In: Nature Reviews. Molecular Cell Biology, Vol. 18, No. 3, 03.2017, p. 141-158.

Research output: Contribution to journalReviewResearchpeer-review

Harvard

Hammond, C, Strømme, CB, Huang, H, Patel, DJ & Groth, A 2017, 'Histone chaperone networks shaping chromatin function', Nature Reviews. Molecular Cell Biology, vol. 18, no. 3, pp. 141-158. https://doi.org/10.1038/nrm.2016.159

APA

Hammond, C., Strømme, C. B., Huang, H., Patel, D. J., & Groth, A. (2017). Histone chaperone networks shaping chromatin function. Nature Reviews. Molecular Cell Biology, 18(3), 141-158. https://doi.org/10.1038/nrm.2016.159

Vancouver

Hammond C, Strømme CB, Huang H, Patel DJ, Groth A. Histone chaperone networks shaping chromatin function. Nature Reviews. Molecular Cell Biology. 2017 Mar;18(3):141-158. https://doi.org/10.1038/nrm.2016.159

Author

Hammond, Colin ; Strømme, Caroline Bianchi ; Huang, Hongda ; Patel, Dinshaw J ; Groth, Anja. / Histone chaperone networks shaping chromatin function. In: Nature Reviews. Molecular Cell Biology. 2017 ; Vol. 18, No. 3. pp. 141-158.

Bibtex

@article{bb7259f8aa97441292c9c6505316e2f5,
title = "Histone chaperone networks shaping chromatin function",
abstract = "The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.",
author = "Colin Hammond and Str{\o}mme, {Caroline Bianchi} and Hongda Huang and Patel, {Dinshaw J} and Anja Groth",
year = "2017",
month = mar,
doi = "10.1038/nrm.2016.159",
language = "English",
volume = "18",
pages = "141--158",
journal = "Nature Reviews. Molecular Cell Biology",
issn = "1471-0072",
publisher = "nature publishing group",
number = "3",

}

RIS

TY - JOUR

T1 - Histone chaperone networks shaping chromatin function

AU - Hammond, Colin

AU - Strømme, Caroline Bianchi

AU - Huang, Hongda

AU - Patel, Dinshaw J

AU - Groth, Anja

PY - 2017/3

Y1 - 2017/3

N2 - The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.

AB - The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.

U2 - 10.1038/nrm.2016.159

DO - 10.1038/nrm.2016.159

M3 - Review

C2 - 28053344

VL - 18

SP - 141

EP - 158

JO - Nature Reviews. Molecular Cell Biology

JF - Nature Reviews. Molecular Cell Biology

SN - 1471-0072

IS - 3

ER -

ID: 174434845