| http://purl.uniprot.org/citations/24214985 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24214985 | http://www.w3.org/2000/01/rdf-schema#comment | "Post-translational histone methylation is a dynamic and reversible process that is involved in the spatio-temporal regulation of gene transcription and contributes to various cellular phenotypes. Methylation of histone H3 at lysine 9 (H3K9), which is generally a transcriptional repression mark, is demethylated by H3K9-specific demethylases, leading to transcriptional activation. However, how multiple demethylases with the same substrate specificity differ in their chromatin targeting mechanisms has not been well understood. Unlike other H3K9-specific demethylases, it has been reported that JMJD1A likely forms a homodimer, but a detailed mode of dimerization and the possible link between structure and enzymatic activity have remained unresolved. Here, we report the structure-function relationship of JMJD1A in detail. First, JMJD1A forms a homodimer through its catalytic domains, bringing the two active sites close together. Second, increasing the concentration of JMJD1A facilitates efficient production of unmethylated product from dimethyl-H3K9 and decreases the release of the monomethylated intermediate. Finally, substituting one of the two active sites with an inactive mutant results in a significant reduction of the demethylation rate without changing the affinity to the intermediate. Given this evidence, we propose a substrate channeling model for the efficient conversion of dimethylated H3K9 into the unmethylated state. Our study provides valuable information that will help in understanding the redundancy of H3K9-specific demethylases and the complementary activity of their unique structures and enzymatic properties for appropriate control of chromatin modification patterns."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.492595"xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/author | "Goda S."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/author | "Kawamura T."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/author | "Aburatani H."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/author | "Isagawa T."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/author | "Chikaoka Y."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/pages | "36948-36956"xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/title | "Control of histone H3 lysine 9 (H3K9) methylation state via cooperative two-step demethylation by Jumonji domain containing 1A (JMJD1A) homodimer."xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://purl.uniprot.org/core/volume | "288"xsd:string |
| http://purl.uniprot.org/citations/24214985 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24214985 |
| http://purl.uniprot.org/citations/24214985 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24214985 |
| http://purl.uniprot.org/uniprot/#_B4E2H5-mappedCitation-24214985 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24214985 |
| http://purl.uniprot.org/uniprot/#_Q9Y4C1-mappedCitation-24214985 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24214985 |
| http://purl.uniprot.org/uniprot/Q9Y4C1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24214985 |
| http://purl.uniprot.org/uniprot/B4E2H5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24214985 |