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Literature DB >> 23525333

A novel role of the N terminus of budding yeast histone H3 variant Cse4 in ubiquitin-mediated proteolysis.

Wei Chun Au¹, Anthony R Dawson, David W Rawson, Sara B Taylor, Richard E Baker, Munira A Basrai.

Abstract

Regulating levels of centromeric histone H3 (CenH3) variant is crucial for genome stability. Interaction of Psh1, an E3 ligase, with the C terminus of Cse4 has been shown to contribute to its proteolysis. Here, we demonstrate a role for ubiquitination of the N terminus of Cse4 in regulating Cse4 proteolysis for faithful chromosome segregation and a role for Doa1 in ubiquitination of Cse4.

Entities: Gene Species

Keywords: Cse4; Doa1; Psh1; chromosome segregation; ubiquitin-mediated protein degradation

Mesh：

Substances：

Year: 2013 PMID： 23525333 PMCID： PMC3664860 DOI： 10.1534/genetics.113.149898

Source DB: PubMed Journal: Genetics ISSN： 0016-6731 Impact factor: 4.562

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