title: Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl Cis-Trans isomerase.
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.
authors: Center for Childhood Cancer, The Research Institute, Nationwide Children's Hospital, Columbus, Ohio 43205.
authors: Kentaro
authors: K
authors: Ohkuni
authors: Rashid
authors: R
authors: Abdulle
authors: Katsumi
authors: K
authors: Kitagawa
mesh_terms: D043171:Chromosomal Instability; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D015825:Chromosomes, Fungal; D004268:DNA-Binding Proteins / Q000378:metabolism*; D020104:Immunophilins / Q000235:genetics / Q000378:metabolism*; D008938:Mitosis; D010445:Peptide Elongation Factors / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D059748:Proteolysis; D012441:Saccharomyces cerevisiae / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: C092746:CSE4 protein, S cerevisiae; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D010445:Peptide Elongation Factors; D029701:Saccharomyces cerevisiae Proteins; C554184:Psh1 protein, S cerevisiae; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex; C403327:FPR3 protein, S cerevisiae; D020104:Immunophilins
keywords: Cse4; Fpr3; Psh1; isomerization; protein degradation