The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

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

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The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. / Bowman, Andrew; Hammond, Colin M; Stirling, Andrew; Ward, Richard; Shang, Weifeng; El Mkami, Hassane; Robinson, David A.; Svergun, Dmitri I.; Norman, David G; Owen-Hughes, Tom.

In: Nucleic Acids Research, Vol. 42, No. 9, 05.2014, p. 6038-51.

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

Harvard

Bowman, A, Hammond, CM, Stirling, A, Ward, R, Shang, W, El Mkami, H, Robinson, DA, Svergun, DI, Norman, DG & Owen-Hughes, T 2014, 'The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution', Nucleic Acids Research, vol. 42, no. 9, pp. 6038-51. https://doi.org/10.1093/nar/gku232

APA

Bowman, A., Hammond, C. M., Stirling, A., Ward, R., Shang, W., El Mkami, H., Robinson, D. A., Svergun, D. I., Norman, D. G., & Owen-Hughes, T. (2014). The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Research, 42(9), 6038-51. https://doi.org/10.1093/nar/gku232

Vancouver

Bowman A, Hammond CM, Stirling A, Ward R, Shang W, El Mkami H et al. The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Research. 2014 May;42(9):6038-51. https://doi.org/10.1093/nar/gku232

Author

Bowman, Andrew ; Hammond, Colin M ; Stirling, Andrew ; Ward, Richard ; Shang, Weifeng ; El Mkami, Hassane ; Robinson, David A. ; Svergun, Dmitri I. ; Norman, David G ; Owen-Hughes, Tom. / The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. In: Nucleic Acids Research. 2014 ; Vol. 42, No. 9. pp. 6038-51.

Bibtex

@article{137aec9690e743bd80a35bd2c93f37bb,
title = "The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution",
abstract = "NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.",
keywords = "Models, Molecular, Molecular Chaperones, Nucleosome Assembly Protein 1, Protein Binding, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Scattering, Small Angle, Solutions, X-Ray Diffraction, Journal Article, Research Support, Non-U.S. Gov't",
author = "Andrew Bowman and Hammond, {Colin M} and Andrew Stirling and Richard Ward and Weifeng Shang and {El Mkami}, Hassane and Robinson, {David A.} and Svergun, {Dmitri I.} and Norman, {David G} and Tom Owen-Hughes",
note = "{\textcopyright} The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2014",
month = may,
doi = "10.1093/nar/gku232",
language = "English",
volume = "42",
pages = "6038--51",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "9",

}

RIS

TY - JOUR

T1 - The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution

AU - Bowman, Andrew

AU - Hammond, Colin M

AU - Stirling, Andrew

AU - Ward, Richard

AU - Shang, Weifeng

AU - El Mkami, Hassane

AU - Robinson, David A.

AU - Svergun, Dmitri I.

AU - Norman, David G

AU - Owen-Hughes, Tom

N1 - © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2014/5

Y1 - 2014/5

N2 - NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.

AB - NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.

KW - Models, Molecular

KW - Molecular Chaperones

KW - Nucleosome Assembly Protein 1

KW - Protein Binding

KW - Protein Interaction Domains and Motifs

KW - Protein Structure, Quaternary

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Scattering, Small Angle

KW - Solutions

KW - X-Ray Diffraction

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1093/nar/gku232

DO - 10.1093/nar/gku232

M3 - Journal article

C2 - 24688059

VL - 42

SP - 6038

EP - 6051

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 9

ER -

ID: 178883218