着丝粒组蛋白H3变体Cse4的降解需要Fpr3肽基脯氨酰顺反异构酶。
Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl Cis-Trans isomerase.
作者信息
Ohkuni Kentaro, Abdulle Rashid, Kitagawa Katsumi
机构信息
Center for Childhood Cancer, The Research Institute, Nationwide Children's Hospital, Columbus, Ohio 43205.
出版信息
Genetics. 2014 Apr;196(4):1041-5. doi: 10.1534/genetics.114.161224. Epub 2014 Feb 10.
Abstract
The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae is polyubiquitylated and degraded in a proteasome-dependent manner. We report here that the proline isomerase Fpr3 regulates Cse4 proteolysis. Structural change in Cse4 by Fpr3 might be important for the interaction between Cse4 and the E3 ubiquitin ligase Psh1.
摘要
酿酒酵母中的着丝粒组蛋白H3变体Cse4会发生多聚泛素化，并以蛋白酶体依赖的方式被降解。我们在此报告脯氨酸异构酶Fpr3调节Cse4的蛋白水解。Fpr3引起的Cse4结构变化可能对Cse4与E3泛素连接酶Psh1之间的相互作用很重要。
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本文引用的文献
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Analysis of protein phosphatase-1 and aurora protein kinase suppressors reveals new aspects of regulatory protein function in Saccharomyces cerevisiae.分析蛋白磷酸酶-1 和极光蛋白激酶抑制剂揭示了酿酒酵母中调节蛋白功能的新方面。
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An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation.Ufd3中的犰狳基序与Cdc48相互作用，并参与泛素稳态和蛋白质降解。
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