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Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron–sulphur cluster metabolism

Identifieur interne : 000093 ( France/Analysis ); précédent : 000092; suivant : 000094

Mitochondrial 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 :

RBID : PMC:3245475

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 Arabidopsis 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 Arabidopsis proteins were validated by in vitro import assays with purified pea organelles and by targeting assays in Arabidopsis 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 Arabidopsis proteins was established by functional complementation of an Escherichia coli COG0354 (ygfZ) deletant; both plant genes restored in vivo activity of the Fe/S enzyme MiaB but restoration was abrogated when folates were eliminated by deleting folP. Insertional inactivation of At4g12130 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.


Url:
DOI: 10.1093/jxb/err286
PubMed: 21984653
PubMed Central: 3245475


Affiliations:


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PMC:3245475

Le document en format XML

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<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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