TY - JOUR
T1 - Multiple E3s promote the degradation of histone H3 variant Cse4
AU - Cheng, Haili
AU - Bao, Xin
AU - Gan, Xin
AU - Luo, Shiwen
AU - Rao, Hai
N1 - Funding Information:
We are grateful to Drs. M. Hochstrasser, R. Deshaies, S. Biggins, M. A. Basrai, R. Verma, C. Wu, J. Wisniewski, D. Morgan and S. Lee for strains and plasmids. We thank Dr. M. Strand for support and members of the Rao laboratory for discussions. H.R. is supported by grants from the National Institutes of Health (GM 118350), the National Center for Advancing Translational Science (UL1TR001120), the William & Ella Owens Medical Research Foundation, and the Department of Defense (W911NF-11-10466).
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
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U2 - 10.1038/s41598-017-08923-w
DO - 10.1038/s41598-017-08923-w
M3 - Article
C2 - 28819127
AN - SCOPUS:85027689960
VL - 7
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
IS - 1
M1 - 8565
ER -