<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(1)</volume><submitter>Matsuura T</submitter><pubmed_abstract>The Cys2/His2-type zinc finger protein Zfp296 has been implicated in stem cell pluripotency and tumor pathogenesis. However, its mechanisms remain elusive. Here, we demonstrated that a Zfp296 deficiency in mice impairs germ-cell development and embryonic growth. Zfp296 was intracellularly localized to heterochromatin in embryos. A GST-Zfp296 pull-down experiment using ES cell nuclear extract followed by LC-MS/MS showed that Zfp296 interacts with component proteins of heterochromatin (such as HP1, Dnmt1, Dnmt3b, and ATRX) and the NuRD complex. We focused on H3K9 methylation as a hallmark of heterochromatin, and found that Zfp296 overexpression in cultured cells reduces the Suv39h1-mediated H3K9 methylation. Consistent with this finding, in Zfp296 &lt;sup>-/-&lt;/sup> mouse embryos, we observed a </pubmed_abstract><journal>Scientific reports</journal><pagination>12462</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5622089</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Zfp296 negatively regulates H3K9 methylation in embryonic development as a component of heterochromatin.</pubmed_title><pmcid>PMC5622089</pmcid><pubmed_authors>Miyazaki JI</pubmed_authors><pubmed_authors>Matsuura T</pubmed_authors><pubmed_authors>Tashiro F</pubmed_authors><pubmed_authors>Miyazaki T</pubmed_authors><pubmed_authors>Miyazaki S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Zfp296 negatively regulates H3K9 methylation in embryonic development as a component of heterochromatin.</name><description>The Cys2/His2-type zinc finger protein Zfp296 has been implicated in stem cell pluripotency and tumor pathogenesis. However, its mechanisms remain elusive. Here, we demonstrated that a Zfp296 deficiency in mice impairs germ-cell development and embryonic growth. Zfp296 was intracellularly localized to heterochromatin in embryos. A GST-Zfp296 pull-down experiment using ES cell nuclear extract followed by LC-MS/MS showed that Zfp296 interacts with component proteins of heterochromatin (such as HP1, Dnmt1, Dnmt3b, and ATRX) and the NuRD complex. We focused on H3K9 methylation as a hallmark of heterochromatin, and found that Zfp296 overexpression in cultured cells reduces the Suv39h1-mediated H3K9 methylation. Consistent with this finding, in Zfp296 &lt;sup>-/-&lt;/sup> mouse embryos, we observed a </description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Sep</publication><modification>2026-05-05T21:21:31.423Z</modification><creation>2019-03-27T02:57:52Z</creation></dates><accession>S-EPMC5622089</accession><cross_references><pubmed>28963472</pubmed><doi>10.1038/s41598-017-12772-y</doi></cross_references></HashMap>