Degradation of Centromeric Histone H3 Variant Cse4 Requires the Fpr3 Peptidyl-prolyl Cis–Trans Isomerase | Zendy

Kentaro Ohkuni | Zendy; Rashid Abdulle | Zendy; Katsumi Kitagawa | Zendy

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Degradation of Centromeric Histone H3 Variant Cse4 Requires the Fpr3 Peptidyl-prolyl Cis–Trans Isomerase

Author(s) -

Kentaro Ohkuni,

Rashid Abdulle,

Katsumi Kitagawa

Publication year - 2014

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.114.161224

Subject(s) - ubiquitin ligase , biology , saccharomyces cerevisiae , ubiquitin , proteolysis , histone h3 , histone , proteasome , histone h2a , genetics , prolyl isomerase , biochemistry , microbiology and biotechnology , isomerase , pin1 , enzyme , dna , yeast , gene

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.

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