Regulation of plant cytosolic aldolase functions by redox-modifications

DC FieldValueLanguage
dc.contributor.authorvan der Linde, Karina
dc.contributor.authorGutsche, Nora
dc.contributor.authorLetters, Hans-Martin
dc.contributor.authorLindermayr, Christian
dc.contributor.authorMueller, Bernd
dc.contributor.authorHoltgrefe, Simone
dc.contributor.authorScheibe, Renate
dc.date.accessioned2021-12-23T16:13:58Z-
dc.date.available2021-12-23T16:13:58Z-
dc.date.issued2011
dc.identifier.issn09819428
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10843-
dc.description.abstractFrom the five genes which code for cytosolic fructose 1,6-bisphosphate aldolases in Arabidopsis thaliana L, the cDNA clone of cAld2 (At2g36460), was heterologously expressed in E. coli and incubated under various oxidizing and reducing conditions. Covalent binding of a GSH moiety to the enzyme was shown by incorporation of biotinylated GSH (BioGEE) and by immunodetection with monoclonal anti-GSH serum. Nitrosylation after incubation with GSNO or SNP was demonstrated using the biotin-switch assay. Mass-spectrometry analysis showed glutathionylation and/or nitrosylation at two different cysteine residues: GSH was found to be attached to C68 and C173, while the nitroso-group was incorporated only into C173. Non-reducing SDS-PAGE conducted with purified wild-type and various Cysmutant proteins revealed the presence of disulfide bridges in the oxidized enzyme, as described for rabbit muscle aldolase. Incubation of the purified enzyme with GSSG (up to 25 mM) led to partial and reversible inactivation of enzyme activity; NADPH, in the presence of the components of the cytosolic NADP-dependent thioredoxin system, could reactivate the aldolase as did DTT. Total and irreversible inactivation occurred with low concentrations (0.1 mM) of nitrosoglutathione (GSNO). Inactivation was prevented by co-incubation of cAld2 with fructose-1,6-bisphosphate (FBP). Nuclear localization of cAld2 and interaction with thioredoxins was shown by transient expression of fusion constructs with fluorescent proteins in isolated protoplasts. (C) 2011 Elsevier Masson SAS. All rights reserved.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [FOR 387, SFB 944, P9]; The authors wish to thank Dr. Stefan Walter, Osnabrueck, for his advice with the ESI-MS analysis, and Bianca Altmann, Christina Wunrau, Ellen Vatterott, Samantha Druce, Malayko MontillaMartinez, and Dagmar Bergholz for help with some of the experiments. Help with figure formatting by Nicolas Konig is greatly appreciated. Thanks are also due to F.J. Cejudo (Sevilla, Spain) for the kind gift of the wheat NTR plasmid. The financial support provided by the Deutsche Forschungsgemeinschaft (FOR 387 and SFB 944, P9) is gratefully acknowledged.
dc.language.isoen
dc.publisherELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
dc.relation.ispartofPLANT PHYSIOLOGY AND BIOCHEMISTRY
dc.subjectArabidopsis thaliana
dc.subjectBiotin-switch assay
dc.subjectCytosolic aldolase
dc.subjectDEHYDROGENASE
dc.subjectDisulfide bridge
dc.subjectGLUTAREDOXINS
dc.subjectGlutathionylation
dc.subjectGSNO
dc.subjectGSSG
dc.subjectIDENTIFICATION
dc.subjectMETABOLIC ENZYMES
dc.subjectMUSCLE FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE
dc.subjectNitrosylation
dc.subjectNuclear localization
dc.subjectNUCLEAR-LOCALIZATION
dc.subjectPlant Sciences
dc.subjectPROTEIN S-GLUTATHIONYLATION
dc.subjectROS
dc.subjectSplit-YFP
dc.subjectSULFHYDRYL-GROUPS
dc.subjectTHIOREDOXIN
dc.subjectThioredoxin h
dc.subjectTRANSCRIPTION
dc.titleRegulation of plant cytosolic aldolase functions by redox-modifications
dc.typejournal article
dc.identifier.doi10.1016/j.plaphy.2011.06.009
dc.identifier.isiISI:000295072800002
dc.description.volume49
dc.description.issue9
dc.description.startpage946
dc.description.endpage957
dc.contributor.orcid0000-0002-9343-4996
dc.contributor.orcid0000-0003-1390-8344
dc.contributor.researcheridM-7338-2014
dc.publisher.place65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE
dcterms.isPartOf.abbreviationPlant Physiol. Biochem.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-6140-6181-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidGuNo208-
crisitem.author.netidScRe288-
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