<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>13</volume><submitter>Folsche V</submitter><pubmed_abstract>Plant tetrapyrrole biosynthesis (TPS) provides the indispensable chlorophyll (Chl) and heme molecules in photosynthetic organisms. Post-translational mechanisms control the enzymes to ensure a balanced flow of intermediates in the pathway and synthesis of appropriate amounts of both endproducts. One of the critical regulators of TPS is GENOMES UNCOUPLED 4 (GUN4). GUN4 interacts with magnesium chelatase (MgCh), and its binding of the catalytic substrate and product of the MgCh reaction stimulates the insertion of Mg&lt;sup>2+&lt;/sup> into protoporphyrin IX. Despite numerous &lt;i>in vitro&lt;/i> studies, knowledge about the &lt;i>in vivo&lt;/i> function of the GUN4:porphyrin interaction for the whole TPS pathway, particularly in plants, is still limited. To address this, we focused on two highly conserved a</pubmed_abstract><journal>Frontiers in plant science</journal><pagination>850504</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8967248</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Impact of Porphyrin Binding to GENOMES UNCOUPLED 4 on Tetrapyrrole Biosynthesis &lt;i>in planta&lt;/i>.</pubmed_title><pmcid>PMC8967248</pmcid><pubmed_authors>Großmann C</pubmed_authors><pubmed_authors>Richter AS</pubmed_authors><pubmed_authors>Folsche V</pubmed_authors></additional><is_claimable>false</is_claimable><name>Impact of Porphyrin Binding to GENOMES UNCOUPLED 4 on Tetrapyrrole Biosynthesis &lt;i>in planta&lt;/i>.</name><description>Plant tetrapyrrole biosynthesis (TPS) provides the indispensable chlorophyll (Chl) and heme molecules in photosynthetic organisms. Post-translational mechanisms control the enzymes to ensure a balanced flow of intermediates in the pathway and synthesis of appropriate amounts of both endproducts. One of the critical regulators of TPS is GENOMES UNCOUPLED 4 (GUN4). GUN4 interacts with magnesium chelatase (MgCh), and its binding of the catalytic substrate and product of the MgCh reaction stimulates the insertion of Mg&lt;sup>2+&lt;/sup> into protoporphyrin IX. Despite numerous &lt;i>in vitro&lt;/i> studies, knowledge about the &lt;i>in vivo&lt;/i> function of the GUN4:porphyrin interaction for the whole TPS pathway, particularly in plants, is still limited. To address this, we focused on two highly conserved a</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022</publication><modification>2025-04-26T15:16:10.29Z</modification><creation>2025-04-06T14:53:17.004Z</creation></dates><accession>S-EPMC8967248</accession><cross_references><pubmed>35371166</pubmed><doi>10.3389/fpls.2022.850504</doi></cross_references></HashMap>