Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis

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

Standard

Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. / Fierz, Beat; Kilic, Sinan; Luger, Karolin; Muir, Tom W.

In: Journal of the American Chemical Society, Vol. 134, No. 48, 05.12.2012, p. 19548-19551.

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

Harvard

Fierz, B, Kilic, S, Luger, K & Muir, TW 2012, 'Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis', Journal of the American Chemical Society, vol. 134, no. 48, pp. 19548-19551. https://doi.org/10.1021/ja308908p

APA

Fierz, B., Kilic, S., Luger, K., & Muir, T. W. (2012). Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. Journal of the American Chemical Society, 134(48), 19548-19551. https://doi.org/10.1021/ja308908p

Vancouver

Fierz B, Kilic S, Luger K, Muir TW. Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. Journal of the American Chemical Society. 2012 Dec 5;134(48):19548-19551. https://doi.org/10.1021/ja308908p

Author

Fierz, Beat ; Kilic, Sinan ; Luger, Karolin ; Muir, Tom W. / Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. In: Journal of the American Chemical Society. 2012 ; Vol. 134, No. 48. pp. 19548-19551.

Bibtex

@article{c0cf247b957e4140bd8b790aa567a59e,
title = "Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis",
abstract = "Post-translational modifications (PTMs) of histones are an essential feature in the dynamic regulation of chromatin. One of these modifications, ubiquitylation, has been speculated to directly influence the stability of the nucleosome, which represents the basic building block of chromatin. Here we report a strategy for the semisynthesis of site-specifically ubiquitylated histone H2A (uH2A). This branched protein was generated through a three-piece expressed protein ligation approach including a traceless ligation at valine. uH2A could be efficiently incorporated into nucleosomes, thereby opening the way to detailed biochemical and biophysical studies on the function of this PTM. Accordingly, we used uH2A, as well as a previously generated ubiquitylated H2B, in chaperone-coupled nucleosome stability assays to demonstrate that the direct effect of ubiquitylated histones on nucleosomal stability is in fact modest.",
author = "Beat Fierz and Sinan Kilic and Karolin Luger and Muir, {Tom W.}",
year = "2012",
month = dec,
day = "5",
doi = "10.1021/ja308908p",
language = "English",
volume = "134",
pages = "19548--19551",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "48",

}

RIS

TY - JOUR

T1 - Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis

AU - Fierz, Beat

AU - Kilic, Sinan

AU - Luger, Karolin

AU - Muir, Tom W.

PY - 2012/12/5

Y1 - 2012/12/5

N2 - Post-translational modifications (PTMs) of histones are an essential feature in the dynamic regulation of chromatin. One of these modifications, ubiquitylation, has been speculated to directly influence the stability of the nucleosome, which represents the basic building block of chromatin. Here we report a strategy for the semisynthesis of site-specifically ubiquitylated histone H2A (uH2A). This branched protein was generated through a three-piece expressed protein ligation approach including a traceless ligation at valine. uH2A could be efficiently incorporated into nucleosomes, thereby opening the way to detailed biochemical and biophysical studies on the function of this PTM. Accordingly, we used uH2A, as well as a previously generated ubiquitylated H2B, in chaperone-coupled nucleosome stability assays to demonstrate that the direct effect of ubiquitylated histones on nucleosomal stability is in fact modest.

AB - Post-translational modifications (PTMs) of histones are an essential feature in the dynamic regulation of chromatin. One of these modifications, ubiquitylation, has been speculated to directly influence the stability of the nucleosome, which represents the basic building block of chromatin. Here we report a strategy for the semisynthesis of site-specifically ubiquitylated histone H2A (uH2A). This branched protein was generated through a three-piece expressed protein ligation approach including a traceless ligation at valine. uH2A could be efficiently incorporated into nucleosomes, thereby opening the way to detailed biochemical and biophysical studies on the function of this PTM. Accordingly, we used uH2A, as well as a previously generated ubiquitylated H2B, in chaperone-coupled nucleosome stability assays to demonstrate that the direct effect of ubiquitylated histones on nucleosomal stability is in fact modest.

UR - http://www.scopus.com/inward/record.url?scp=84870708220&partnerID=8YFLogxK

U2 - 10.1021/ja308908p

DO - 10.1021/ja308908p

M3 - Journal article

C2 - 23163596

AN - SCOPUS:84870708220

VL - 134

SP - 19548

EP - 19551

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 48

ER -

ID: 280237507