Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl cis-trans isomerase

Kentaro Ohkuni; Rashid Abdulle; Katsumi Kitagawa

doi:10.1534/genetics.114.161224

Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl cis-trans isomerase

Kentaro Ohkuni, Rashid Abdulle, Katsumi Kitagawa

Producción científica: Article › revisión exhaustiva

26 Citas (Scopus)

Resumen

The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae is polyubiquitylated and degraded in a proteasomedependent 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.

Idioma original	English (US)
Páginas (desde-hasta)	1041-1045
Número de páginas	5
Publicación	Genetics
Volumen	196
N.º	4
DOI	https://doi.org/10.1534/genetics.114.161224
Estado	Published - abr 2014
Publicado de forma externa	Sí

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General Medicine

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abstract = "The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae is polyubiquitylated and degraded in a proteasomedependent 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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AB - The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae is polyubiquitylated and degraded in a proteasomedependent 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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Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl cis-trans isomerase

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