- -

Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts

RiuNet: Institutional repository of the Polithecnic University of Valencia

Share/Send to

Cited by

Statistics

  • Estadisticas de Uso

Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts

Show simple item record

Files in this item

dc.contributor.author Sanz-Barrio, Ruth es_ES
dc.contributor.author Fernandez-San Millan, Alicia es_ES
dc.contributor.author Corral Martínez, Patricia es_ES
dc.contributor.author Seguí-Simarro, Jose M. es_ES
dc.contributor.author Farran, Inmaculada es_ES
dc.date.accessioned 2016-11-09T12:08:29Z
dc.date.available 2016-11-09T12:08:29Z
dc.date.issued 2011-08
dc.identifier.issn 1467-7644
dc.identifier.uri http://hdl.handle.net/10251/73664
dc.description.abstract Thioredoxins (Trxs) are small ubiquitous disulphide proteins widely known to enhance expression and solubility of recombinant proteins in microbial expression systems. Given the common evolutionary heritage of chloroplasts and bacteria, we attempted to analyse whether plastid Trxs could also act as modulators of recombinant protein expression in transgenic chloroplasts. For that purpose, two tobacco Trxs (m and f) with different phylogenetic origins were assessed. Using plastid transformation, we assayed two strategies: the fusion and the co-expression of Trxs with human serum albumin (HSA), which was previously observed to form large protein bodies in tobacco chloroplasts. Our results indicate that both Trxs behave similarly as regards HSA accumulation, although they act differently when fused or co-expressed with HSA. Trxs-HSA fusions markedly increased the final yield of HSA (up to 26% of total protein) when compared with control lines that only expressed HSA; this increase was mainly caused by higher HSA stability of the fused proteins. However, the fusion strategy failed to prevent the formation of protein bodies within chloroplasts. On the other hand, the co-expression constructs gave rise to an absence of large protein bodies although no more soluble HSA was accumulated. In these plants, electron micrographs showed HSA and Trxs co-localization in small protein bodies with fibrillar texture, suggesting a possible influence of Trxs on HSA solubilization. Moreover, the in vitro chaperone activity of Trx m and f was demonstrated, which supports the hypothesis of a direct relationship between Trx presence and HSA aggregates solubilization in plants co-expressing both proteins. © 2011 The Authors. Plant Biotechnology Journal © 2011 Society for Experimental Biology, Association of Applied Biologists and Blackwell Publishing Ltd. es_ES
dc.description.sponsorship Authors wish to thank MJ Villafranca for excellent plant care and cultivation. This work was supported by grants Res. 17/2004 and IIM10865.RI1 (Proyecto EUROINNOVA) from Gobierno de Navarra (Spain). RSB and PCM were supported by predoctoral fellowships from CSIC and Generalitat Valenciana, respectively. AFS was supported by a postdoctoral fellowship from Public University of Navarra. en_EN
dc.language Inglés es_ES
dc.publisher Wiley es_ES
dc.relation.ispartof Plant Biotechnology Journal es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Human serum albumin es_ES
dc.subject Plastid transformation es_ES
dc.subject Thioredoxin es_ES
dc.subject Tobacco es_ES
dc.subject Chaperone es_ES
dc.subject Hybrid protein es_ES
dc.subject Serum albumin es_ES
dc.subject Article es_ES
dc.subject Biosynthesis es_ES
dc.subject Chloroplast es_ES
dc.subject Genetic transformation es_ES
dc.subject Genetics es_ES
dc.subject Metabolism es_ES
dc.subject Plasmid es_ES
dc.subject Plastid es_ES
dc.subject Solubility es_ES
dc.subject Transgenic plant es_ES
dc.subject Chloroplast Thioredoxins es_ES
dc.subject Chloroplasts es_ES
dc.subject Molecular Chaperones es_ES
dc.subject Plants, Genetically Modified es_ES
dc.subject Plasmids es_ES
dc.subject Plastids es_ES
dc.subject Recombinant Fusion Proteins es_ES
dc.subject Transformation, Genetic es_ES
dc.subject Bacteria (microorganisms) es_ES
dc.subject Nicotiana tabacum es_ES
dc.subject.classification GENETICA es_ES
dc.title Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1111/j.1467-7652.2011.00608.x
dc.relation.projectID info:eu-repo/grantAgreement/Gobierno de Navarra//IIM10865.RI1/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario de Conservación y Mejora de la Agrodiversidad Valenciana - Institut Universitari de Conservació i Millora de l'Agrodiversitat Valenciana es_ES
dc.contributor.affiliation Universitat Politècnica de València. Escuela Técnica Superior de Ingeniería Agronómica y del Medio Natural - Escola Tècnica Superior d'Enginyeria Agronòmica i del Medi Natural es_ES
dc.description.bibliographicCitation Sanz-Barrio, R.; Fernandez-San Millan, A.; Corral Martínez, P.; Seguí-Simarro, JM.; Farran, I. (2011). Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts. Plant Biotechnology Journal. 9(6):639-650. https://doi.org/10.1111/j.1467-7652.2011.00608.x es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion https://dx.doi.org/10.1111/j.1467-7652.2011.00608.x es_ES
dc.description.upvformatpinicio 639 es_ES
dc.description.upvformatpfin 650 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 9 es_ES
dc.description.issue 6 es_ES
dc.relation.senia 198309 es_ES
dc.contributor.funder Gobierno de Navarra es_ES
dc.contributor.funder Consejo Superior de Investigaciones Científicas es_ES
dc.contributor.funder Generalitat Valenciana es_ES
dc.contributor.funder Universidad Pública de Navarra es_ES


This item appears in the following Collection(s)

Show simple item record