Sulfurtransferase and thioredoxin specifically interact as demonstrated by bimolecular fluorescence complementation analysis and biochemical tests

DC FieldValueLanguage
dc.contributor.authorHenne, Melina
dc.contributor.authorKoenig, Nicolas
dc.contributor.authorTriulzi, Tiziana
dc.contributor.authorBaroni, Sara
dc.contributor.authorForlani, Fabio
dc.contributor.authorScheibe, Renate
dc.contributor.authorPapenbrock, Jutta
dc.date.accessioned2021-12-23T16:15:59Z-
dc.date.available2021-12-23T16:15:59Z-
dc.date.issued2015
dc.identifier.issn22115463
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11672-
dc.description.abstractSulfurtransferases (Strs) and thioredoxins (Trxs) are members of large protein families. Trxs are disulfide reductases and play an important role in redox-related cellular processes. They interact with a broad range of proteins. Strs catalyze the transfer of a sulfur atom from a suitable sulfur donor to nucleophilic sulfur acceptors in vitro, but the physiological roles of these enzymes are not well defined. Several studies in different organisms demonstrate protein-protein interactions of Strs with members of the Trx family. We are interested in investigating the specificity of the interaction between Str and Trx isoforms. In order to use the bimolecular fluorescence complementation (BiFC), several Str and Trx sequences from Arabidopsis thaliana were cloned into the pUC-SPYNE and pUC-SPYCE split-YFP vectors, respectively. Each couple of plasmids containing the sequences for the putative interaction partners were transformed into Arabidopsis protoplasts and screened using a confocal laser scanning microscope. Compartment-and partner-specific interactions could be observed in transformed protoplasts. Replacement of cysteine residues in the redox-active site of Trxs abolished the interaction signal. Therefore, the redox site is not only involved in the redox reaction but also responsible for the interaction with partner proteins. Biochemical assays support a specific interaction among Strs and certain Trxs. Based on the results obtained, the interaction of Strs and Trxs indicates a role of Strs in the maintenance of the cellular redox homeostasis. (C) 2015 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. This is an open access article under the CC BY-NC-ND license.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [PA 764/1-4, PA 764/1-5]; Universita degli Studi di Milano; DAADDeutscher Akademischer Austausch Dienst (DAAD)European Commission [Vigoni 0815171]; We would like to thank Pamela von Trzebiatowski and Silke Walter for their excellent technical assistance. Anshu Kuriakose, Vellore, India, produced some of the mutant thioredoxin clones as a part of her MSc thesis. We acknowledge the gift of recombinant thioredoxin proteins for initial biochemical analysis from Yves Meyer, Perpignan, France, and the gift of split-YFP vectors from Klaus Harter, Tubingen, Germany. The project was originally started in cooperation with Simone Holtgrefe, Osnabruck, and Divya Bagchi, Jabalpur, India. Christian Boestfleisch, Hannover, helped to improve Fig. 2. The work was supported financially by grants from the Deutsche Forschungsgemeinschaft to J.P. (PA 764/1-4 and 1-5), by the Universita degli Studi di Milano to T.T., and by the DAAD (Vigoni 0815171).
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofFEBS OPEN BIO
dc.subjectARABIDOPSIS
dc.subjectArabidopsis thaliana
dc.subjectBimolecular fluorescence complementation
dc.subjectBiochemistry & Molecular Biology
dc.subjectIDENTIFICATION
dc.subjectMERCAPTOPYRUVATE SULFURTRANSFERASE
dc.subjectMOLECULAR-MECHANISMS
dc.subjectPLANTS
dc.subjectProtein interaction
dc.subjectPROTEIN-PROTEIN INTERACTIONS
dc.subjectREDOX
dc.subjectRHODANESE
dc.subjectSYSTEM
dc.subjectThioredoxin
dc.subjectVISUALIZATION
dc.titleSulfurtransferase and thioredoxin specifically interact as demonstrated by bimolecular fluorescence complementation analysis and biochemical tests
dc.typejournal article
dc.identifier.doi10.1016/j.fob.2015.10.001
dc.identifier.isiISI:000366999300101
dc.description.volume5
dc.description.startpage832
dc.description.endpage843
dc.contributor.orcid0000-0003-3050-8676
dc.contributor.orcid0000-0001-9405-973X
dc.contributor.researcheridC-1070-2017
dc.contributor.researcheridY-4265-2019
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationFEBS Open Bio
dcterms.oaStatusGreen Published, gold
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-6140-6181-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidScRe288-
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