The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes. / Hammond, Colin M; Sundaramoorthy, Ramasubramanian; Larance, Mark; Lamond, Angus; Stevens, Michael A; El Mkami, Hassane; Norman, David G; Owen-Hughes, Tom.

In: Nucleic Acids Research, Vol. 44, No. 13, 27.07.2016, p. 6157-72.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hammond, CM, Sundaramoorthy, R, Larance, M, Lamond, A, Stevens, MA, El Mkami, H, Norman, DG & Owen-Hughes, T 2016, 'The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes', Nucleic Acids Research, vol. 44, no. 13, pp. 6157-72. https://doi.org/10.1093/nar/gkw209

APA

Hammond, C. M., Sundaramoorthy, R., Larance, M., Lamond, A., Stevens, M. A., El Mkami, H., Norman, D. G., & Owen-Hughes, T. (2016). The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes. Nucleic Acids Research, 44(13), 6157-72. https://doi.org/10.1093/nar/gkw209

Vancouver

Hammond CM, Sundaramoorthy R, Larance M, Lamond A, Stevens MA, El Mkami H et al. The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes. Nucleic Acids Research. 2016 Jul 27;44(13):6157-72. https://doi.org/10.1093/nar/gkw209

Author

Hammond, Colin M ; Sundaramoorthy, Ramasubramanian ; Larance, Mark ; Lamond, Angus ; Stevens, Michael A ; El Mkami, Hassane ; Norman, David G ; Owen-Hughes, Tom. / The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes. In: Nucleic Acids Research. 2016 ; Vol. 44, No. 13. pp. 6157-72.

Bibtex

@article{11ec79ba5a0f412981bef1e431860030,
title = "The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes",
abstract = "Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.",
keywords = "Journal Article",
author = "Hammond, {Colin M} and Ramasubramanian Sundaramoorthy and Mark Larance and Angus Lamond and Stevens, {Michael A} and {El Mkami}, Hassane and Norman, {David G} and Tom Owen-Hughes",
note = "{\textcopyright} The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2016",
month = jul,
day = "27",
doi = "10.1093/nar/gkw209",
language = "English",
volume = "44",
pages = "6157--72",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "13",

}

RIS

TY - JOUR

T1 - The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes

AU - Hammond, Colin M

AU - Sundaramoorthy, Ramasubramanian

AU - Larance, Mark

AU - Lamond, Angus

AU - Stevens, Michael A

AU - El Mkami, Hassane

AU - Norman, David G

AU - Owen-Hughes, Tom

N1 - © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2016/7/27

Y1 - 2016/7/27

N2 - Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.

AB - Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.

KW - Journal Article

U2 - 10.1093/nar/gkw209

DO - 10.1093/nar/gkw209

M3 - Journal article

C2 - 27036862

VL - 44

SP - 6157

EP - 6172

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 13

ER -

ID: 178883095