期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 291, 期 19, 页码 10372-10377出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M115.701813
关键词
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资金
- Welch Foundation [AQ 1747]
- William AMP
- Ella Owens Medical Research Foundation
- Helen F. Kerr Foundation
- Department of Defense [W911NF-11-10466]
- National Institutes of Health [GM 078085]
Cse4, a histone H3-like centromeric protein, plays critical functions in chromosome segregation. Cse4 level is tightly regulated, but the underlying mechanism remains poorly understood. We employed a toxicity-based screen to look for the degradation components involved in Cse4 regulation. Here, we show that the F-box containing protein Rcy1 is required for efficient Cse4 turnover as Cse4 degradation is compromised in yeast cells lacking RCY1. Excessive Cse4 accumulation in rcy1 Delta cells leads to growth retardation. Furthermore, the deletion of RCY1 is tied to enhanced chromosome instability and temperature-sensitive cell growth. Our results reveal the involvement of Rcy1 in chromosome regulation and another regulatory pathway controlling the Cse4 level and activity.
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