Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron-sulphur cluster metabolism.
Identifieur interne : 002989 ( Main/Exploration ); précédent : 002988; suivant : 002990Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron-sulphur cluster metabolism.
Auteurs : Jeffrey C. Waller [États-Unis] ; Kenneth W. Ellens ; Sophie Alvarez ; Karen Loizeau ; Stéphane Ravanel ; Andrew D. HansonSource :
- Journal of experimental botany [ 1460-2431 ] ; 2012.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Fer (métabolisme), Mitochondries (métabolisme), Phylogenèse (MeSH), Plastes (métabolisme), Protéines d'Arabidopsis (composition chimique), Protéines d'Arabidopsis (métabolisme), Similitude de séquences d'acides aminés (MeSH), Soufre (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Protéines d'Arabidopsis.
- métabolisme : Fer, Mitochondries, Plastes, Protéines d'Arabidopsis, Soufre.
- Données de séquences moléculaires, Phylogenèse, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Arabidopsis Proteins.
- chemical , metabolism : Arabidopsis Proteins, Iron, Sulfur.
- metabolism : Mitochondria, Plastids.
- Amino Acid Sequence, Molecular Sequence Data, Phylogeny, Sequence Homology, Amino Acid.
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.
DOI: 10.1093/jxb/err286
PubMed: 21984653
PubMed Central: PMC3245475
Affiliations:
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Ellens</name></author><author><name sortKey="Alvarez, Sophie" sort="Alvarez, Sophie" uniqKey="Alvarez S" first="Sophie" last="Alvarez">Sophie Alvarez</name></author><author><name sortKey="Loizeau, Karen" sort="Loizeau, Karen" uniqKey="Loizeau K" first="Karen" last="Loizeau">Karen Loizeau</name></author><author><name sortKey="Ravanel, Stephane" sort="Ravanel, Stephane" uniqKey="Ravanel S" first="Stéphane" last="Ravanel">Stéphane Ravanel</name></author><author><name sortKey="Hanson, Andrew D" sort="Hanson, Andrew D" uniqKey="Hanson A" first="Andrew D" last="Hanson">Andrew D. Hanson</name></author></analytic><series><title level="j">Journal of experimental botany</title><idno type="eISSN">1460-2431</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (metabolism)</term><term>Iron (metabolism)</term><term>Mitochondria (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Plastids (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires (MeSH)</term><term>Fer (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Phylogenèse (MeSH)</term><term>Plastes (métabolisme)</term><term>Protéines d'Arabidopsis (composition chimique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Soufre (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Iron</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines d'Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Plastids</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term><term>Mitochondries</term><term>Plastes</term><term>Protéines d'Arabidopsis</term><term>Soufre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Phylogenèse</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21984653</PMID><DateCompleted><Year>2012</Year><Month>04</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2431</ISSN><JournalIssue CitedMedium="Internet"><Volume>63</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Journal of experimental botany</Title><ISOAbbreviation>J Exp Bot</ISOAbbreviation></Journal><ArticleTitle>Mitochondrial and plastidial COG0354 proteins have folate-dependent functions in iron-sulphur cluster metabolism.</ArticleTitle><Pagination><MedlinePgn>403-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/err286</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Waller</LastName><ForeName>Jeffrey C</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Horticultural Sciences Department, University of Florida, Gainesville, FL 32611, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ellens</LastName><ForeName>Kenneth W</ForeName><Initials>KW</Initials></Author><Author ValidYN="Y"><LastName>Alvarez</LastName><ForeName>Sophie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Loizeau</LastName><ForeName>Karen</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Ravanel</LastName><ForeName>Stéphane</ForeName><Initials>S</Initials></Author><Author 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IdType="pubmed">19402753</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Floride</li></region></list><tree><noCountry><name sortKey="Alvarez, Sophie" sort="Alvarez, Sophie" uniqKey="Alvarez S" first="Sophie" last="Alvarez">Sophie Alvarez</name><name sortKey="Ellens, Kenneth W" sort="Ellens, Kenneth W" uniqKey="Ellens K" first="Kenneth W" last="Ellens">Kenneth W. Ellens</name><name sortKey="Hanson, Andrew D" sort="Hanson, Andrew D" uniqKey="Hanson A" first="Andrew D" last="Hanson">Andrew D. Hanson</name><name sortKey="Loizeau, Karen" sort="Loizeau, Karen" uniqKey="Loizeau K" first="Karen" last="Loizeau">Karen Loizeau</name><name sortKey="Ravanel, Stephane" sort="Ravanel, Stephane" uniqKey="Ravanel S" first="Stéphane" last="Ravanel">Stéphane Ravanel</name></noCountry><country name="États-Unis"><region name="Floride"><name sortKey="Waller, Jeffrey C" sort="Waller, Jeffrey C" uniqKey="Waller J" first="Jeffrey C" last="Waller">Jeffrey C. Waller</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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