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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2017-08-01
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Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-017-08923-w |
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doaj-51778c3d13ec488b907e80f30c51fb762020-12-08T00:37:33ZengNature Publishing GroupScientific Reports2045-23222017-08-01711810.1038/s41598-017-08923-wMultiple E3s promote the degradation of histone H3 variant Cse4Haili Cheng0Xin Bao1Xin Gan2Shiwen Luo3Hai Rao4Department of Molecular Medicine, The University of Texas Health Science CenterDepartment of Molecular Medicine, The University of Texas Health Science CenterResearch Institute of Respiratory Medicine, The First Affiliated Hospital, Nanchang UniversityCenter for Experimental Medicine, The First Affiliated Hospital, Nanchang UniversityDepartment of Molecular Medicine, The University of Texas Health Science CenterAbstract 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.https://doi.org/10.1038/s41598-017-08923-w |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Haili Cheng Xin Bao Xin Gan Shiwen Luo Hai Rao |
spellingShingle |
Haili Cheng Xin Bao Xin Gan Shiwen Luo Hai Rao Multiple E3s promote the degradation of histone H3 variant Cse4 Scientific Reports |
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 Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2017-08-01 |
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. |
url |
https://doi.org/10.1038/s41598-017-08923-w |
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