http://purl.uniprot.org/citations/19223465 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19223465 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/19223465 | http://www.w3.org/2000/01/rdf-schema#comment | "PR-Set7/Set8/KMT5A is the sole enzyme known to catalyze monomethylation of histone H4 lysine 20 (H4K20) and is present only in multicellular organisms that compact a large fraction of their DNA. We found that mouse embryos that are homozygous null mutants for the gene PR-Set7 display early embryonic lethality prior to the eight-cell stage. Death was due to the absence of PR-Set7 catalytic activity, since microinjection of the wild type, but not a catalytically inactive version, into two-cell embryos rescued the phenotype. A lack of PR-Set7 activity resulted not only in depletion of H4K20me1 but also in reduced levels of the H4K20me2/3 marks catalyzed by the Suv4-20h1/h2 enzymes, implying that H4K20me1 may be essential for the function of these enzymes to ensure the dimethylated and trimethylated states. Embryonic stem cells that were inducibly deleted for PR-Set7 passed through an initial G(2)/M phase, but the progeny were defective at the subsequent S and G(2)/M phases, exhibiting a delay in their cell cycle, accumulation at G(2)/M, massive DNA damage, and improper mitotic chromosome condensation. Cell cycle analysis after synchronization indicated that the defects were a consequence of decreased H4K20me1 due to the absence of PR-Set7. Most importantly, the lack of H4K20me1 also resulted in defects in chromosome condensation in interphase nuclei. These results demonstrate the critical role of H4K20 monomethylation in mammals in a developmental context."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.01768-08"xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Chu J."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Oda H."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Reinberg D."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Heard E."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Shen M.M."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Torres-Padilla M.E."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Okamoto I."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Murphy N."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/author | "Price S.M."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/pages | "2278-2295"xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/title | "Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development."xsd:string |
http://purl.uniprot.org/citations/19223465 | http://purl.uniprot.org/core/volume | "29"xsd:string |
http://purl.uniprot.org/citations/19223465 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19223465 |
http://purl.uniprot.org/citations/19223465 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19223465 |
http://purl.uniprot.org/citations/19223465 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19223465 |
http://purl.uniprot.org/citations/19223465 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19223465 |
http://purl.uniprot.org/enzyme/2.1.1.361 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19223465 |
http://purl.uniprot.org/uniprot/#_A0A0G2JGZ8-mappedCitation-19223465 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19223465 |
http://purl.uniprot.org/uniprot/#_D3YXI6-mappedCitation-19223465 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19223465 |