<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>62(11)</volume><submitter>Xiang L</submitter><pubmed_abstract>Over the past decades, considerable advances have been made in understanding the crucial role and the regulation of sucrose metabolism in plants. Among the various sucrose-catabolizing enzymes, alkaline/neutral invertases (A/N-Invs) have long remained poorly studied. However, recent findings have demonstrated the presence of A/N-Invs in various organelles in addition to the cytosol, and their importance for plant development and stress tolerance. A cytosolic (At-A/N-InvG, At1g35580) and a mitochondrial (At-A/N-InvA, At1g56560) member of the A/N-Invs have been analysed in more detail in Arabidopsis and it was found that At-A/N-InvA knockout plants show an even more severe growth phenotype than At-A/N-InvG knockout plants. The absence of either A/N-Inv was associated with higher oxidative stress defence gene expression, while transient overexpression of At-A/N-InvA and At-A/N-InvG in leaf mesophyll protoplasts down-regulated the oxidative stress-responsive ascorbate peroxidase 2 (APX2) promoter. Moreover, up-regulation of the APX2 promoter by hydrogen peroxide or abscisic acid could be blocked by adding metabolizable sugars or ascorbate. A hypothetical model is proposed in which both mitochondrial and cytosolic A/N-Invs can generate glucose as a substrate for mitochondria-associated hexokinase, contributing to mitochondrial reactive oxygen species homeostasis.</pubmed_abstract><journal>Journal of experimental botany</journal><pagination>3849-62</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3134342</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Exploring the neutral invertase-oxidative stress defence connection in Arabidopsis thaliana.</pubmed_title><pmcid>PMC3134342</pmcid><pubmed_authors>Bolouri-Moghaddam MR</pubmed_authors><pubmed_authors>Le Roy K</pubmed_authors><pubmed_authors>Lammens W</pubmed_authors><pubmed_authors>Rolland F</pubmed_authors><pubmed_authors>Vanhaecke M</pubmed_authors><pubmed_authors>Van den Ende W</pubmed_authors><pubmed_authors>Xiang L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Exploring the neutral invertase-oxidative stress defence connection in Arabidopsis thaliana.</name><description>Over the past decades, considerable advances have been made in understanding the crucial role and the regulation of sucrose metabolism in plants. Among the various sucrose-catabolizing enzymes, alkaline/neutral invertases (A/N-Invs) have long remained poorly studied. However, recent findings have demonstrated the presence of A/N-Invs in various organelles in addition to the cytosol, and their importance for plant development and stress tolerance. A cytosolic (At-A/N-InvG, At1g35580) and a mitochondrial (At-A/N-InvA, At1g56560) member of the A/N-Invs have been analysed in more detail in Arabidopsis and it was found that At-A/N-InvA knockout plants show an even more severe growth phenotype than At-A/N-InvG knockout plants. The absence of either A/N-Inv was associated with higher oxidative stress defence gene expression, while transient overexpression of At-A/N-InvA and At-A/N-InvG in leaf mesophyll protoplasts down-regulated the oxidative stress-responsive ascorbate peroxidase 2 (APX2) promoter. Moreover, up-regulation of the APX2 promoter by hydrogen peroxide or abscisic acid could be blocked by adding metabolizable sugars or ascorbate. A hypothetical model is proposed in which both mitochondrial and cytosolic A/N-Invs can generate glucose as a substrate for mitochondria-associated hexokinase, contributing to mitochondrial reactive oxygen species homeostasis.</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Jul</publication><modification>2025-04-27T02:16:36.783Z</modification><creation>2019-03-27T03:06:59Z</creation></dates><accession>S-EPMC3134342</accession><cross_references><pubmed>21441406</pubmed><doi>10.1093/jxb/err069</doi></cross_references></HashMap>