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Thioredoxin Selectivity for Thiol-based Redox Regulation of Target Proteins in Chloroplasts

Yoshida, Keisuke ; Hara, Satoshi ; Hisabori, Toru

The Journal of biological chemistry, 2015-06, Vol.290 (23), p.14278-14288 [Periódico revisado por pares]

United States: Elsevier Inc

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  • Título:
    Thioredoxin Selectivity for Thiol-based Redox Regulation of Target Proteins in Chloroplasts
  • Autor: Yoshida, Keisuke ; Hara, Satoshi ; Hisabori, Toru
  • Assuntos: Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - metabolism ; Arabidopsis Proteins - metabolism ; chloroplast ; Chloroplasts - metabolism ; enzyme ; enzyme mechanism ; NADP - metabolism ; Oxidation-Reduction ; Plant Biology ; plant physiology ; Recombinant Proteins - metabolism ; redox regulation ; Sulfhydryl Compounds - metabolism ; thiol ; thioredoxin ; Thioredoxins - metabolism
  • É parte de: The Journal of biological chemistry, 2015-06, Vol.290 (23), p.14278-14288
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: Redox regulation based on the thioredoxin (Trx) system is believed to ensure light-responsive control of various functions in chloroplasts. Five Trx subtypes have been reported to reside in chloroplasts, but their functional diversity in the redox regulation of Trx target proteins remains poorly clarified. To directly address this issue, we studied the Trx-dependent redox shifts of several chloroplast thiol-modulated enzymes in vitro and in vivo. In vitro assays using a series of Arabidopsis recombinant proteins provided new insights into Trx selectivity for the redox regulation as well as the underpinning for previous suggestions. Most notably, by combining the discrimination of thiol status with mass spectrometry and activity measurement, we identified an uncharacterized aspect of the reductive activation of NADP-malate dehydrogenase; two redox-active Cys pairs harbored in this enzyme were reduced via distinct utilization of Trxs even within a single polypeptide. In our in vitro assays, Trx-f was effective in reducing all thiol-modulated enzymes analyzed here. We then investigated the in vivo physiological relevance of these in vitro findings, using Arabidopsis wild-type and Trx-f-deficient plants. Photoreduction of fructose-1,6-bisphosphatase was partially impaired in Trx-f-deficient plants, but the global impact of Trx-f deficiency on the redox behaviors of thiol-modulated enzymes was not as striking as expected from the in vitro data. Our results provide support for the in vivo functionality of the Trx system and also highlight the complexity and plasticity of the chloroplast redox network. Background: Thioredoxin (Trx) plays a pivotal role in the redox regulation of target proteins. Results: Functional diversity of chloroplast Trxs was determined by observing Trx-dependent redox shifts of several thiol-modulated enzymes in vitro and in vivo. Conclusion: Novel insights into the chloroplast redox network were provided. Significance: Our results shed light on the molecular basis of the light-responsive adjustment of chloroplast functions.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
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