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http://purl.uniprot.org/citations/23706739http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23706739http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23706739http://www.w3.org/2000/01/rdf-schema#comment"Histone acetylation plays critical roles in chromatin remodeling, DNA repair, and epigenetic regulation of gene expression, but the underlying mechanisms are unclear. Proteasomes usually catalyze ATP- and polyubiquitin-dependent proteolysis. Here, we show that the proteasomes containing the activator PA200 catalyze the polyubiquitin-independent degradation of histones. Most proteasomes in mammalian testes ("spermatoproteasomes") contain a spermatid/sperm-specific α subunit α4 s/PSMA8 and/or the catalytic β subunits of immunoproteasomes in addition to PA200. Deletion of PA200 in mice abolishes acetylation-dependent degradation of somatic core histones during DNA double-strand breaks and delays core histone disappearance in elongated spermatids. Purified PA200 greatly promotes ATP-independent proteasomal degradation of the acetylated core histones, but not polyubiquitinated proteins. Furthermore, acetylation on histones is required for their binding to the bromodomain-like regions in PA200 and its yeast ortholog, Blm10. Thus, PA200/Blm10 specifically targets the core histones for acetylation-mediated degradation by proteasomes, providing mechanisms by which acetylation regulates histone degradation, DNA repair, and spermatogenesis."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.04.032"xsd:string
http://purl.uniprot.org/citations/23706739http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.04.032"xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Cheng Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Cheng Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Cao C."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Cao C."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Goldberg A.L."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Goldberg A.L."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Komatsu T."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Komatsu T."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Liu S."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Pang Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Pang Y."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Song W."xsd:string
http://purl.uniprot.org/citations/23706739http://purl.uniprot.org/core/author"Song W."xsd:string