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Identification of uricase as a potential target of plant thioredoxin: Implication in the regulation of nodule development

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dc.contributor.authorDu, Hui-
dc.contributor.authorKim, Sunghan-
dc.contributor.authorNam, Kyoung Hee-
dc.contributor.authorLee, Myung-Sok-
dc.contributor.authorSon, Ora-
dc.contributor.authorLee, Suk-Ha-
dc.contributor.authorCheon, Choong-Ill-
dc.date.available2021-02-22T13:47:43Z-
dc.date.created2020-09-01-
dc.date.issued2010-06-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/13185-
dc.description.abstractDuring symbiotic nodule development in legume roots, early signaling events between host and rhizobia serve critical determinants for the proper onset of nodule morphogenesis, nitrogen fixation, and assimilation. Previously we isolated thioredoxin from soybean nodules as one of differentially expressed genes during nodulation and noted its positive role in nitrogen fixation. To identify the target proteins of thioredoxin in nodules, we used thioredoxin affinity chromatography followed by mass spectrometry. Nodulin-35, a subunit of uricase, was found to be a target of thioredoxin. Their interaction was confirmed by pull-down assay and by bimolecular fluorescent complementation. With an increased uricase activity observed also in the presence of thioredoxin, these results appear to implicate a novel role of thioredoxin in the regulation of enzyme activities involved in nodule development and nitrogen fixation. (C) 2010 Elsevier Inc. All rights reserved.-
dc.language영어-
dc.language.isoen-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.titleIdentification of uricase as a potential target of plant thioredoxin: Implication in the regulation of nodule development-
dc.typeArticle-
dc.contributor.affiliatedAuthorNam, Kyoung Hee-
dc.contributor.affiliatedAuthorLee, Myung-Sok-
dc.contributor.affiliatedAuthorSon, Ora-
dc.contributor.affiliatedAuthorCheon, Choong-Ill-
dc.identifier.doi10.1016/j.bbrc.2010.05.040-
dc.identifier.scopusid2-s2.0-77953617288-
dc.identifier.wosid000279292800005-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.397, no.1, pp.22 - 26-
dc.relation.isPartOfBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume397-
dc.citation.number1-
dc.citation.startPage22-
dc.citation.endPage26-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.subject.keywordPlusESCHERICHIA-COLI-
dc.subject.keywordPlusROOT-NODULES-
dc.subject.keywordPlusUNINFECTED CELLS-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusPEROXISOMES-
dc.subject.keywordPlusMITOCHONDRIA-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusNODULIN-35-
dc.subject.keywordPlusAPOPTOSIS-
dc.subject.keywordPlusTRANSPORT-
dc.subject.keywordAuthorThioredoxin-
dc.subject.keywordAuthorNodulin-35-
dc.subject.keywordAuthorUricase-
dc.subject.keywordAuthorNodule development-
dc.identifier.urlhttps://www.sciencedirect.com/science/article/abs/pii/S0006291X10009319?via%3Dihub-
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