A Novel Role of the N Terminus of Budding Yeast Histone H3 Variant Cse4 in Ubiquitin-Mediated Proteolysis | Zendy

Wei-Chun Au | Zendy; Anthony R. Dawson | Zendy; David W Rawson | Zendy; Sara B. Taylor | Zendy; Richard E. Baker | Zendy; Munira A. Basrai | Zendy

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A Novel Role of the N Terminus of Budding Yeast Histone H3 Variant Cse4 in Ubiquitin-Mediated Proteolysis

Author(s) -

Wei-Chun Au,

Anthony R. Dawson,

David W Rawson,

Sara B. Taylor,

Richard E. Baker,

Munira A. Basrai

Publication year - 2013

Publication title -

genetics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.792

H-Index - 246

eISSN - 1943-2631

pISSN - 0016-6731

DOI - 10.1534/genetics.113.149898

Subject(s) - ubiquitin ligase , proteolysis , biology , ubiquitin , histone , genetics , microbiology and biotechnology , budding yeast , histone h2a , saccharomyces cerevisiae , cell division control protein 4 , histone h3 , yeast , dna , biochemistry , gene , enzyme

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.

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