OrangerV1, France, Analysis, bibRecord, 000178

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase

Identifieur interne : 000178 ( France/Analysis ); précédent : 000177; suivant : 000179

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase

Auteurs : Eric Gelhaye ; Nicolas Rouhier ; Joelle Gérard [France] ; Yves Jolivet [France] ; José Gualberto [France] ; Nicolas Navrot ; Per-Ingvard Ohlsson [Suède] ; Gunnar Wingsle [Suède] ; Masakazu Hirasawa [États-Unis] ; David B. Knaff [États-Unis] ; Hongmei Wang ; Pierre Dizengremel [France] ; Yves Meyer [France] ; Jean-Pierre Jacquot

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.

RBID : PMC:521959

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.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC521959

DOI: 10.1073/pnas.0405282101
PubMed: 15385674
PubMed Central: 521959

Affiliations:

Links to Exploration step

PMC:521959

Le document en format XML

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<series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
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<front><div type="abstract" xml:lang="en"><p>The plant mitochondrial thioredoxin (Trx) system has been described as containing an NADPH-dependent Trx reductase and Trx <italic>o</italic>
. In addition to the mitochondrial isoform, Trx <italic>o</italic>
, plants are known to contain several chloroplastic Trx isoforms and the cytosolic Trx <italic>h</italic>
 isoforms. We report here the presence in plant mitochondria of a Trx isoform (PtTrx<italic>h</italic>
2) belonging to the Trx <italic>h</italic>
 group. Western blot analyses with mitochondrial proteins isolated from both poplar and GFP fusion constructs indicate that PtTrx<italic>h</italic>
2 is targeted to plant mitochondria. The recombinant protein, PtTrx<italic>h</italic>
2, has been shown to be reduced efficiently by the mitochondrial Trx reductase AtNTRA. PtTrx<italic>h</italic>
2 is also able to reduce alternative oxidase homodimers and to allow its activation by pyruvate. In contrast, neither PtTrx<italic>h</italic>
2 nor AtTrx<italic>o</italic>
1 exhibits activity with several poplar glutathione peroxidases and especially a putative mitochondrial isoform. Incubation of PtTrx<italic>h</italic>
2 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 PtTrx<italic>h</italic>
2 from -290 to -225 mV. In addition to Trx <italic>o</italic>
, this study shows that Trx <italic>h</italic>
 could also be present in mitochondria. This previously unrecognized complexity is not unexpected, considering the multiple redox-regulated processes found in plant mitochondria.</p>
</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
<li>Suède</li>
<li>États-Unis</li>
</country>
<region><li>Alsace (région administrative)</li>
<li>Grand Est</li>
<li>Languedoc-Roussillon</li>
<li>Lorraine (région)</li>
<li>Occitanie (région administrative)</li>
<li>Texas</li>
</region>
<settlement><li>Perpignan</li>
<li>Strasbourg</li>
<li>Vandoeuvre</li>
</settlement>
<orgName><li>Université Henri Poincaré</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
<name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name>
<name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name>
<name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
<name sortKey="Wang, Hongmei" sort="Wang, Hongmei" uniqKey="Wang H" first="Hongmei" last="Wang">Hongmei Wang</name>
</noCountry>
<country name="France"><region name="Grand Est"><name sortKey="Gerard, Joelle" sort="Gerard, Joelle" uniqKey="Gerard J" first="Joelle" last="Gérard">Joelle Gérard</name>
</region>
<name sortKey="Dizengremel, Pierre" sort="Dizengremel, Pierre" uniqKey="Dizengremel P" first="Pierre" last="Dizengremel">Pierre Dizengremel</name>
<name sortKey="Gualberto, Jose" sort="Gualberto, Jose" uniqKey="Gualberto J" first="José" last="Gualberto">José Gualberto</name>
<name sortKey="Jolivet, Yves" sort="Jolivet, Yves" uniqKey="Jolivet Y" first="Yves" last="Jolivet">Yves Jolivet</name>
<name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</name>
</country>
<country name="Suède"><noRegion><name sortKey="Ohlsson, Per Ingvard" sort="Ohlsson, Per Ingvard" uniqKey="Ohlsson P" first="Per-Ingvard" last="Ohlsson">Per-Ingvard Ohlsson</name>
</noRegion>
<name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name>
</country>
<country name="États-Unis"><region name="Texas"><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name>
</region>
<name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B." last="Knaff">David B. Knaff</name>
</country>
</tree>
</affiliations>
</record>

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A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase

A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase

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