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The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation

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The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation. / Bowman, Andrew; Ward, Richard; Wiechens, Nicola; Singh, Vijender; El Mkami, Hassane; Norman, David George; Owen-Hughes, Tom.

In: Molecular Cell, Vol. 41, No. 4, 18.02.2011, p. 398-408.

Research output: Contribution to journalArticle

Harvard

Bowman, A, Ward, R, Wiechens, N, Singh, V, El Mkami, H, Norman, DG & Owen-Hughes, T 2011, 'The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation', Molecular Cell, vol. 41, no. 4, pp. 398-408. https://doi.org/10.1016/j.molcel.2011.01.025

APA

Bowman, A., Ward, R., Wiechens, N., Singh, V., El Mkami, H., Norman, D. G., & Owen-Hughes, T. (2011). The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation. Molecular Cell, 41(4), 398-408. https://doi.org/10.1016/j.molcel.2011.01.025

Vancouver

Bowman A, Ward R, Wiechens N, Singh V, El Mkami H, Norman DG et al. The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation. Molecular Cell. 2011 Feb 18;41(4):398-408. https://doi.org/10.1016/j.molcel.2011.01.025

Author

Bowman, Andrew ; Ward, Richard ; Wiechens, Nicola ; Singh, Vijender ; El Mkami, Hassane ; Norman, David George ; Owen-Hughes, Tom. / The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation. In: Molecular Cell. 2011 ; Vol. 41, No. 4. pp. 398-408.

Bibtex - Download

@article{67702c4503c04e94a5c3d9560189a345,
title = "The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation",
abstract = "Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.",
keywords = "NUCLEOSOME ASSEMBLY PROTEIN-1, DNA-REPLICATION, ACETYLTRANSFERASE RTT109, CRYSTAL-STRUCTURE, STRUCTURAL BASIS, COMPLEXES, CORE, CHROMATIN, ACETYLATION, ASF1",
author = "Andrew Bowman and Richard Ward and Nicola Wiechens and Vijender Singh and {El Mkami}, Hassane and Norman, {David George} and Tom Owen-Hughes",
year = "2011",
month = "2",
day = "18",
doi = "10.1016/j.molcel.2011.01.025",
language = "English",
volume = "41",
pages = "398--408",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4 in a Tetrameric Conformation

AU - Bowman, Andrew

AU - Ward, Richard

AU - Wiechens, Nicola

AU - Singh, Vijender

AU - El Mkami, Hassane

AU - Norman, David George

AU - Owen-Hughes, Tom

PY - 2011/2/18

Y1 - 2011/2/18

N2 - Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.

AB - Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.

KW - NUCLEOSOME ASSEMBLY PROTEIN-1

KW - DNA-REPLICATION

KW - ACETYLTRANSFERASE RTT109

KW - CRYSTAL-STRUCTURE

KW - STRUCTURAL BASIS

KW - COMPLEXES

KW - CORE

KW - CHROMATIN

KW - ACETYLATION

KW - ASF1

U2 - 10.1016/j.molcel.2011.01.025

DO - 10.1016/j.molcel.2011.01.025

M3 - Article

VL - 41

SP - 398

EP - 408

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -

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