Thurow, Corinna

[["dc.bibliographiccitation.journal","BMC Plant Biology"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Huang, Li-Jun"],["dc.contributor.author","Li, Ning"],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Wirtz, Markus"],["dc.contributor.author","Hell, Ruediger"],["dc.contributor.author","Gatz, Christiane"],["dc.date.accessioned","2018-11-07T10:08:35Z"],["dc.date.available","2018-11-07T10:08:35Z"],["dc.date.issued","2016"],["dc.description.abstract","Background: Glutaredoxins (GRXs) are small proteins which bind glutathione to either reduce disulfide bonds or to coordinate iron sulfur clusters. Whereas these well-established functions are associated with ubiquitously occurring GRXs that encode variants of a CPYC or a CGFS motif in the active center, land plants also possess CCxC/S-type GRXs (named ROXYs) for which the biochemical functions are yet unknown. ROXYs physically and genetically interact with bZIP transcription factors of the TGA family. In Arabidopsis, ectopically expressed ROXY19 (originally named GRX480 or GRXC9) negatively regulates expression of jasmonic acid/ethylene-induced defense genes through an unknown mechanism that requires at least one of the redundant transcription factors TGA2, TGA5 or TGA6. Results: Ectopically expressed ROXY19 interferes with the activation of TGA-dependent detoxification genes. Similar to the tga2 tga5 tga6 mutant, 35S: ROXY19 plants are more susceptible to the harmful chemical TIBA (2,3,5-triiodobenzoic acid). The repressive function of ROXY19 depends on the integrity of the active site, which can be either CCMC or CPYC but not SSMS. Ectopic expression of the related GRX ROXY18/GRXS13 also led to increased susceptibility to TIBA, indicating potential functional redundancy of members of the ROXY gene family. This redundancy might explain why roxy19 knock-out plants did not show a phenotype with respect to the regulation of the TIBA-induced detoxification program. Complementation of the tga2 tga5 tga6 mutant with either TGA5 or TGA5(C186S), in which the single potential target-site of ROXY19 had been eliminated, did not reveal any evidence for a critical redox modification that might be important for controlling the detoxification program. Conclusions: ROXY19 and related proteins of the ROXY gene family can function as negative regulators of TGA-dependent promoters controlling detoxification genes."],["dc.description.sponsorship","University of Gottingen; German Research Foundation [SPP1710]"],["dc.identifier.doi","10.1186/s12870-016-0886-1"],["dc.identifier.isi","000382908800001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13883"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39488"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1471-2229"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Ectopically expressed glutaredoxin ROXY19 negatively regulates the detoxification pathway in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1532"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Li, Ning"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Huang, Li-Jun"],["dc.contributor.author","Gatz, Christiane"],["dc.date.accessioned","2020-12-10T18:46:59Z"],["dc.date.available","2020-12-10T18:46:59Z"],["dc.date.issued","2019"],["dc.description.sponsorship","the National Natural Science Foundation of China"],["dc.identifier.doi","10.3390/cells8121532"],["dc.identifier.eissn","2073-4409"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78605"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2073-4409"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Reconstitution of the Jasmonate Signaling Pathway in Plant Protoplasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","218"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms"],["dc.bibliographiccitation.lastpage","226"],["dc.bibliographiccitation.volume","1860"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Huang, Li-Jun"],["dc.contributor.author","Barghahn, Sina"],["dc.contributor.author","Willmer, Moritz"],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Gatz, Christiane"],["dc.date.accessioned","2018-11-07T10:27:58Z"],["dc.date.available","2018-11-07T10:27:58Z"],["dc.date.issued","2017"],["dc.description.abstract","Glutaredoxins (GRXs) are small proteins which bind glutathione to either reduce disulfide bonds or to coordinate iron sulfur clusters. Whereas these well-established functions are associated with ubiquitously occurring GRXs that encode variants of a CPYC or a CGFS motif in the active center, land plants also possess CCxC/S-type GRXs (named ROXYs in Arabidopsis thaliana) for which the biochemical functions are yet unknown. ROXYs and CC type GRXs from rice and maize physically and genetically interact with bZIP transcription factors of the TGA family to control developmental and stress-associated processes. Here we demonstrate that ROXYs interact with transcriptional co-repressors of the TOPLESS (TPL) family which are related to Tup1 in fungi and GrouchoffLE in animals. In ROXYs, the functionally important conserved A(L/I)W(L/V) motif at the very C terminus mediates the interaction with TPL. A ternary TGA2/ROXY19/TPL complex is formed when all three proteins are co expressed in yeast. Loss-of-function evidence for the role of TPL in ROXY19-mediated repression was hampered by the redundancy of the five members of the TPL gene family and developmental defects of higher order tpl mutants. As an alternative strategy, we ectopically expressed known TPL-interacting proteins in order to out compete the amount of available TPL in transiently transformed protoplasts. Indeed, ROXY19-mediated transcriptional repression was strongly alleviated by this approach. Our data suggest a yet unrecognized function of GRXs acting as adapter proteins for the assembly of transcriptional repressor complexes on TGA-regulated target promoters. (C) 2016 Published by Elsevier B.V."],["dc.identifier.doi","10.1016/j.bbagrm.2016.11.001"],["dc.identifier.isi","000394072900005"],["dc.identifier.pmid","27838237"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43326"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0006-3002"],["dc.relation.issn","1874-9399"],["dc.title","CC-type glutaredoxins recruit the transcriptional co-repressor TOPLESS to TGA-dependent target promoters in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]