<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(7)</volume><submitter>Li B</submitter><pubmed_abstract>Histone H3-lysine(9) (H3K9) trimethyltransferase gene Su(var) 3-9 was cloned and identified in three Spodoptera insects, Spodopterafrugiperda (S. frugiperda), S. exigua and S. litura. Sequence analysis showed that Spodoptera Su(var) 3-9 is highly conserved evolutionarily. Su(var) 3-9 protein was found to be localized in the nucleus in Sf9 cells, and interact with histone H3, and the heterochromatin protein 1a (HP1a) and HP1b. A dose-dependent enzymatic activity was found at both 27 °C and 37 °C in vitro, with higher activity at 27 °C. Addition of specific inhibitor chaetocin resulted in decreased histone methylation level and host chromatin relaxation. In contrast, overexpression of Su(var) 3-9 caused increased histone methylation level and cellular genome compaction. In AcMNV-infected Sf9</pubmed_abstract><journal>PloS one</journal><pagination>e69442</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3722159</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Identification and characterization of the Spodoptera Su(var) 3-9 histone H3K9 trimethyltransferase and its effect in AcMNPV infection.</pubmed_title><pmcid>PMC3722159</pmcid><pubmed_authors>Li S</pubmed_authors><pubmed_authors>Li B</pubmed_authors><pubmed_authors>Zhong J</pubmed_authors><pubmed_authors>Yin J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification and characterization of the Spodoptera Su(var) 3-9 histone H3K9 trimethyltransferase and its effect in AcMNPV infection.</name><description>Histone H3-lysine(9) (H3K9) trimethyltransferase gene Su(var) 3-9 was cloned and identified in three Spodoptera insects, Spodopterafrugiperda (S. frugiperda), S. exigua and S. litura. Sequence analysis showed that Spodoptera Su(var) 3-9 is highly conserved evolutionarily. Su(var) 3-9 protein was found to be localized in the nucleus in Sf9 cells, and interact with histone H3, and the heterochromatin protein 1a (HP1a) and HP1b. A dose-dependent enzymatic activity was found at both 27 °C and 37 °C in vitro, with higher activity at 27 °C. Addition of specific inhibitor chaetocin resulted in decreased histone methylation level and host chromatin relaxation. In contrast, overexpression of Su(var) 3-9 caused increased histone methylation level and cellular genome compaction. In AcMNV-infected Sf9</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013</publication><modification>2025-04-04T08:00:50.804Z</modification><creation>2019-03-26T23:15:12Z</creation></dates><accession>S-EPMC3722159</accession><cross_references><pubmed>23894480</pubmed><doi>10.1371/journal.pone.0069442</doi></cross_references></HashMap>