A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase. Gelhaye, E., Rouhier, N., Gérard, J., Jolivet, Y., Gualberto, J., Navrot, N., Ohlsson, P., Wingsle, G., Hirasawa, M., Knaff, D. B., Wang, H., Dizengremel, P., Meyer, Y., & Jacquot, J. Proceedings of the National Academy of Sciences, 101(40):14545–14550, October, 2004. Publisher: National Academy of Sciences Section: Biological Sciences![A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.
@article{gelhaye_specific_2004,
title = {A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase},
volume = {101},
copyright = {Copyright © 2004, The National Academy of Sciences},
issn = {0027-8424, 1091-6490},
url = {https://www.pnas.org/content/101/40/14545},
doi = {10/bhgv8p},
abstract = {The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx o. In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.},
language = {en},
number = {40},
urldate = {2021-06-15},
journal = {Proceedings of the National Academy of Sciences},
author = {Gelhaye, Eric and Rouhier, Nicolas and Gérard, Joelle and Jolivet, Yves and Gualberto, José and Navrot, Nicolas and Ohlsson, Per-Ingvard and Wingsle, Gunnar and Hirasawa, Masakazu and Knaff, David B. and Wang, Hongmei and Dizengremel, Pierre and Meyer, Yves and Jacquot, Jean-Pierre},
month = oct,
year = {2004},
pmid = {15385674},
note = {Publisher: National Academy of Sciences
Section: Biological Sciences},
keywords = {glutathione peroxidase, glutathionylation, poplar, redox potential},
pages = {14545--14550},
}
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In addition to the mitochondrial isoform, Trx o, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx h isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrxh2) belonging to the Trx h group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrxh2 is targeted to plant mitochondria. The recombinant protein, PtTrxh2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrxh2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrxh2 nor AtTrxo1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrxh2 with glutathione disulfide led to the formation of glutathionylated Trx, identified by mass spectrometry. The formation of a glutathione adduct increases the redox potential of PtTrxh2 from -290 to -225 mV. In addition to Trx o, this study shows that Trx h could also be present in mitochondria. 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