<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yue Y</submitter><funding>General Program of National Natural Science Foundation of China</funding><funding>Fundamental Research Funds for the Central Universities</funding><funding>National Key R&amp;D Program of China</funding><funding>Fundamental Research Program of Hubei Province</funding><funding>Self-Innovation Fund of Huazhong Agricultural University</funding><funding>National Natural Science Foundation of China Youth Program</funding><funding>Start-up Foundation of Hubei Hongshan Laboratory</funding><pagination>e13169</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12849889</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(5)</volume><pubmed_abstract>SAGA (Spt-Ada-Gcn5 acetyltransferase) is a highly conserved histone acetyltransferase (HAT) complex in eukaryotes, playing a crucial role in regulating gene transcription during development. The complex consists of two core components: GCN5, the HAT subunit, and ADA2, which primarily functions as an adaptor and enhances the complex HAT activity. Beyond its well-established roles, it is discovered in this work that ADA2 in rice possesses a broadly existing intrinsically disordered region (IDR) that directs the formation of nuclear condensates. Moreover, ADA2 is found to interact with a subunit of ATP-citrate lyase (ACL), an enzyme that produces acetyl-CoA, leading to the formation of a GCN5-ADA2-ACL (GAA) complex. ADA2 promotes the condensation of both GCN5 and ACL in vivo. Within these con</pubmed_abstract><journal>Advanced science (Weinheim, Baden-Wurttemberg, Germany)</journal><pubmed_title>ADA2 Forms Nuclear Condensates with GCN5 and ATP-Citrate Lyase (ACL) to Modulate H3K9 Acetylation at Genes Functioning in Rice Meristems.</pubmed_title><pmcid>PMC12849889</pmcid><funding_grant_id>2024AFE001</funding_grant_id><funding_grant_id>2024YFF1000302</funding_grant_id><funding_grant_id>2023hsqd003</funding_grant_id><funding_grant_id>32572255</funding_grant_id><funding_grant_id>2662025SKPY002</funding_grant_id><funding_grant_id>2662025SKPY007</funding_grant_id><funding_grant_id>32300462</funding_grant_id><pubmed_authors>Lai X</pubmed_authors><pubmed_authors>Guo J</pubmed_authors><pubmed_authors>Guo X</pubmed_authors><pubmed_authors>Zhou S</pubmed_authors><pubmed_authors>Lu T</pubmed_authors><pubmed_authors>Lv S</pubmed_authors><pubmed_authors>Abdalla HAM</pubmed_authors><pubmed_authors>Liu B</pubmed_authors><pubmed_authors>Zhou DX</pubmed_authors><pubmed_authors>Zhang R</pubmed_authors><pubmed_authors>Yue Y</pubmed_authors><pubmed_authors>Zhao Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>ADA2 Forms Nuclear Condensates with GCN5 and ATP-Citrate Lyase (ACL) to Modulate H3K9 Acetylation at Genes Functioning in Rice Meristems.</name><description>SAGA (Spt-Ada-Gcn5 acetyltransferase) is a highly conserved histone acetyltransferase (HAT) complex in eukaryotes, playing a crucial role in regulating gene transcription during development. The complex consists of two core components: GCN5, the HAT subunit, and ADA2, which primarily functions as an adaptor and enhances the complex HAT activity. Beyond its well-established roles, it is discovered in this work that ADA2 in rice possesses a broadly existing intrinsically disordered region (IDR) that directs the formation of nuclear condensates. Moreover, ADA2 is found to interact with a subunit of ATP-citrate lyase (ACL), an enzyme that produces acetyl-CoA, leading to the formation of a GCN5-ADA2-ACL (GAA) complex. ADA2 promotes the condensation of both GCN5 and ACL in vivo. Within these con</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Jan</publication><modification>2026-06-13T05:23:51.519Z</modification><creation>2026-06-13T03:08:46.653Z</creation></dates><accession>S-EPMC12849889</accession><cross_references><pubmed>41221643</pubmed><doi>10.1002/advs.202513169</doi></cross_references></HashMap>