Multiple E3s promote the degradation of histone H3 variant Cse4

Abstract The histone H3-like protein Cse4/CENP-A acts as a key molecular marker that differentiates the special centromeric chromatin structures from bulk nucleosomes. As altered Cse4/CENP-A activity leads to genome instability, it is pivotal to understand the mechanism underlying Cse4 regulation. H...

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Autores principales:	Haili Cheng, Xin Bao, Xin Gan, Shiwen Luo, Hai Rao
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/51778c3d13ec488b907e80f30c51fb76
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spelling	oai:doaj.org-article:51778c3d13ec488b907e80f30c51fb762021-12-02T16:06:02ZMultiple E3s promote the degradation of histone H3 variant Cse410.1038/s41598-017-08923-w2045-2322https://doaj.org/article/51778c3d13ec488b907e80f30c51fb762017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08923-whttps://doaj.org/toc/2045-2322Abstract The histone H3-like protein Cse4/CENP-A acts as a key molecular marker that differentiates the special centromeric chromatin structures from bulk nucleosomes. As altered Cse4/CENP-A activity leads to genome instability, it is pivotal to understand the mechanism underlying Cse4 regulation. Here, we demonstrate that four ubiquitin ligases (i.e., Ubr1, Slx5, Psh1, and Rcy1) work in parallel to promote Cse4 turnover in yeast. Interestingly, Cse4 overexpression leads to cellular toxicity and cell cycle delay in yeast cells lacking PSH1, but not in cells lacking UBR1, suggesting different roles of these two degradation pathways. Our findings suggest that various ubiquitin ligases collaborate to keep the Cse4 level in check, providing a basis for further delineating the intricate network involved in Cse4 regulation.Haili ChengXin BaoXin GanShiwen LuoHai RaoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Haili Cheng Xin Bao Xin Gan Shiwen Luo Hai Rao Multiple E3s promote the degradation of histone H3 variant Cse4
description	Abstract The histone H3-like protein Cse4/CENP-A acts as a key molecular marker that differentiates the special centromeric chromatin structures from bulk nucleosomes. As altered Cse4/CENP-A activity leads to genome instability, it is pivotal to understand the mechanism underlying Cse4 regulation. Here, we demonstrate that four ubiquitin ligases (i.e., Ubr1, Slx5, Psh1, and Rcy1) work in parallel to promote Cse4 turnover in yeast. Interestingly, Cse4 overexpression leads to cellular toxicity and cell cycle delay in yeast cells lacking PSH1, but not in cells lacking UBR1, suggesting different roles of these two degradation pathways. Our findings suggest that various ubiquitin ligases collaborate to keep the Cse4 level in check, providing a basis for further delineating the intricate network involved in Cse4 regulation.
format	article
author	Haili Cheng Xin Bao Xin Gan Shiwen Luo Hai Rao
author_facet	Haili Cheng Xin Bao Xin Gan Shiwen Luo Hai Rao
author_sort	Haili Cheng
title	Multiple E3s promote the degradation of histone H3 variant Cse4
title_short	Multiple E3s promote the degradation of histone H3 variant Cse4
title_full	Multiple E3s promote the degradation of histone H3 variant Cse4
title_fullStr	Multiple E3s promote the degradation of histone H3 variant Cse4
title_full_unstemmed	Multiple E3s promote the degradation of histone H3 variant Cse4
title_sort	multiple e3s promote the degradation of histone h3 variant cse4
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/51778c3d13ec488b907e80f30c51fb76
work_keys_str_mv	AT hailicheng multiplee3spromotethedegradationofhistoneh3variantcse4 AT xinbao multiplee3spromotethedegradationofhistoneh3variantcse4 AT xingan multiplee3spromotethedegradationofhistoneh3variantcse4 AT shiwenluo multiplee3spromotethedegradationofhistoneh3variantcse4 AT hairao multiplee3spromotethedegradationofhistoneh3variantcse4
_version_	1718385146332184576

Multiple E3s promote the degradation of histone H3 variant Cse4

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