Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron–sulphur cluster metabolism
Identifieur interne : 001691 ( Main/Exploration ); précédent : 001690; suivant : 001692Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron–sulphur cluster metabolism
Auteurs : Jeffrey C. Waller [États-Unis] ; Kenneth W. Ellens [États-Unis] ; Sophie Alvarez [États-Unis] ; Karen Loizeau [France] ; Stéphane Ravanel [France] ; Andrew D. Hanson [États-Unis]Source :
- Journal of Experimental Botany [ 0022-0957 ] ; 2011.
Abstract
COG0354 proteins have been implicated in synthesis or repair of iron/sulfur (Fe/S) clusters in all domains of life, and those of bacteria, animals, and protists have been shown to require a tetrahydrofolate to function. Two COG0354 proteins were identified in
Url:
DOI: 10.1093/jxb/err286
PubMed: 21984653
PubMed Central: 3245475
Affiliations:
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<series><title level="j">Journal of Experimental Botany</title>
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<front><div type="abstract" xml:lang="en"><p>COG0354 proteins have been implicated in synthesis or repair of iron/sulfur (Fe/S) clusters in all domains of life, and those of bacteria, animals, and protists have been shown to require a tetrahydrofolate to function. Two COG0354 proteins were identified in <italic>Arabidopsis</italic>
and many other plants, one (At4g12130) related to those of α-proteobacteria and predicted to be mitochondrial, the other (At1g60990) related to those of cyanobacteria and predicted to be plastidial. Grasses and poplar appear to lack the latter. The predicted subcellular locations of the <italic>Arabidopsis</italic>
proteins were validated by <italic>in vitro</italic>
import assays with purified pea organelles and by targeting assays in <italic>Arabidopsis</italic>
and tobacco protoplasts using green fluorescent protein fusions. The At4g12130 protein was shown to be expressed mainly in flowers, siliques, and seeds, whereas the At1g60990 protein was expressed mainly in young leaves. The folate dependence of both <italic>Arabidopsis</italic>
proteins was established by functional complementation of an <italic>Escherichia coli COG0354</italic>
(<italic>ygfZ</italic>
) deletant; both plant genes restored <italic>in vivo</italic>
activity of the Fe/S enzyme MiaB but restoration was abrogated when folates were eliminated by deleting <italic>folP</italic>
. Insertional inactivation of <italic>At4g12130</italic>
was embryo lethal; this phenotype was reversed by genetic complementation of the mutant. These data establish that COG0354 proteins have a folate-dependent function in mitochondria and plastids, and that the mitochondrial protein is essential. That plants retain mitochondrial and plastidial COG0354 proteins with distinct phylogenetic origins emphasizes how deeply the extant Fe/S cluster assembly machinery still reflects the ancient endosymbioses that gave rise to plants.</p>
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</TEI>
<affiliations><list><country><li>France</li>
<li>États-Unis</li>
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<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Grenoble</li>
</settlement>
<orgName><li>Université Joseph Fourier</li>
</orgName>
</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Waller, Jeffrey C" sort="Waller, Jeffrey C" uniqKey="Waller J" first="Jeffrey C." last="Waller">Jeffrey C. Waller</name>
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<name sortKey="Alvarez, Sophie" sort="Alvarez, Sophie" uniqKey="Alvarez S" first="Sophie" last="Alvarez">Sophie Alvarez</name>
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<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Loizeau, Karen" sort="Loizeau, Karen" uniqKey="Loizeau K" first="Karen" last="Loizeau">Karen Loizeau</name>
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