Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.
Identifieur interne : 000555 ( Main/Exploration ); précédent : 000554; suivant : 000556Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.
Auteurs : James N. Vranish [États-Unis] ; William K. Russell ; Lusa E. Yu ; Rachael M. Cox ; David H. Russell ; David P. BarondeauSource :
- Journal of the American Chemical Society [ 1520-5126 ] ; 2015.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cinétique (MeSH), Colorants fluorescents (analyse), Colorants fluorescents (composition chimique), Dithiothréitol (composition chimique), Dithiothréitol (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Fluorescence (MeSH), Voies de biosynthèse (MeSH).
- MESH :
- analyse : Colorants fluorescents.
- composition chimique : Colorants fluorescents, Dithiothréitol, Ferrosulfoprotéines.
- métabolisme : Dithiothréitol, Ferrosulfoprotéines.
- Catalyse, Cinétique, Fluorescence, Voies de biosynthèse.
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Fluorescent Dyes.
- chemical , chemistry : Dithiothreitol, Fluorescent Dyes, Iron-Sulfur Proteins.
- chemical , metabolism : Dithiothreitol, Iron-Sulfur Proteins.
- Biosynthetic Pathways, Catalysis, Fluorescence, Kinetics.
Abstract
Iron-sulfur (Fe-S) clusters are protein cofactors that are constructed and delivered to target proteins by elaborate biosynthetic machinery. Mechanistic insights into these processes have been limited by the lack of sensitive probes for tracking Fe-S cluster synthesis and transfer reactions. Here we present fusion protein- and intein-based fluorescent labeling strategies that can probe Fe-S cluster binding. The fluorescence is sensitive to different cluster types ([2Fe-2S] and [4Fe-4S] clusters), ligand environments ([2Fe-2S] clusters on Rieske, ferredoxin (Fdx), and glutaredoxin), and cluster oxidation states. The power of this approach is highlighted with an extreme example in which the kinetics of Fe-S cluster transfer reactions are monitored between two Fdx molecules that have identical Fe-S spectroscopic properties. This exchange reaction between labeled and unlabeled Fdx is catalyzed by dithiothreitol (DTT), a result that was confirmed by mass spectrometry. DTT likely functions in a ligand substitution reaction that generates a [2Fe-2S]-DTT species, which can transfer the cluster to either labeled or unlabeled Fdx. The ability to monitor this challenging cluster exchange reaction indicates that real-time Fe-S cluster incorporation can be tracked for a specific labeled protein in multicomponent assays that include several unlabeled Fe-S binding proteins or other chromophores. Such advanced kinetic experiments are required to untangle the intricate networks of transfer pathways and the factors affecting flux through branch points. High sensitivity and suitability with high-throughput methodology are additional benefits of this approach. We anticipate that this cluster detection methodology will transform the study of Fe-S cluster pathways and potentially other metal cofactor biosynthetic pathways.
DOI: 10.1021/ja510998s
PubMed: 25478817
PubMed Central: PMC4675328
Affiliations:
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Vranish</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Biophysics and ‡Department of Chemistry, Texas A&M University , College Station, Texas 77842-3012, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Biophysics and ‡Department of Chemistry, Texas A&M University , College Station, Texas 77842-3012</wicri:regionArea><wicri:noRegion>Texas 77842-3012</wicri:noRegion></affiliation></author><author><name sortKey="Russell, William K" sort="Russell, William K" uniqKey="Russell W" first="William K" last="Russell">William K. Russell</name></author><author><name sortKey="Yu, Lusa E" sort="Yu, Lusa E" uniqKey="Yu L" first="Lusa E" last="Yu">Lusa E. Yu</name></author><author><name sortKey="Cox, Rachael M" sort="Cox, Rachael M" uniqKey="Cox R" first="Rachael M" last="Cox">Rachael M. Cox</name></author><author><name sortKey="Russell, David H" sort="Russell, David H" uniqKey="Russell D" first="David H" last="Russell">David H. Russell</name></author><author><name sortKey="Barondeau, David P" sort="Barondeau, David P" uniqKey="Barondeau D" first="David P" last="Barondeau">David P. Barondeau</name></author></analytic><series><title level="j">Journal of the American Chemical Society</title><idno type="eISSN">1520-5126</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biosynthetic Pathways (MeSH)</term><term>Catalysis (MeSH)</term><term>Dithiothreitol (chemistry)</term><term>Dithiothreitol (metabolism)</term><term>Fluorescence (MeSH)</term><term>Fluorescent Dyes (analysis)</term><term>Fluorescent Dyes (chemistry)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Kinetics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Colorants fluorescents (analyse)</term><term>Colorants fluorescents (composition chimique)</term><term>Dithiothréitol (composition chimique)</term><term>Dithiothréitol (métabolisme)</term><term>Ferrosulfoprotéines (composition chimique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Fluorescence (MeSH)</term><term>Voies de biosynthèse (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Fluorescent Dyes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dithiothreitol</term><term>Fluorescent Dyes</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dithiothreitol</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Colorants fluorescents</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Colorants fluorescents</term><term>Dithiothréitol</term><term>Ferrosulfoprotéines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dithiothréitol</term><term>Ferrosulfoprotéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosynthetic Pathways</term><term>Catalysis</term><term>Fluorescence</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Cinétique</term><term>Fluorescence</term><term>Voies de biosynthèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron-sulfur (Fe-S) clusters are protein cofactors that are constructed and delivered to target proteins by elaborate biosynthetic machinery. Mechanistic insights into these processes have been limited by the lack of sensitive probes for tracking Fe-S cluster synthesis and transfer reactions. Here we present fusion protein- and intein-based fluorescent labeling strategies that can probe Fe-S cluster binding. The fluorescence is sensitive to different cluster types ([2Fe-2S] and [4Fe-4S] clusters), ligand environments ([2Fe-2S] clusters on Rieske, ferredoxin (Fdx), and glutaredoxin), and cluster oxidation states. The power of this approach is highlighted with an extreme example in which the kinetics of Fe-S cluster transfer reactions are monitored between two Fdx molecules that have identical Fe-S spectroscopic properties. This exchange reaction between labeled and unlabeled Fdx is catalyzed by dithiothreitol (DTT), a result that was confirmed by mass spectrometry. DTT likely functions in a ligand substitution reaction that generates a [2Fe-2S]-DTT species, which can transfer the cluster to either labeled or unlabeled Fdx. The ability to monitor this challenging cluster exchange reaction indicates that real-time Fe-S cluster incorporation can be tracked for a specific labeled protein in multicomponent assays that include several unlabeled Fe-S binding proteins or other chromophores. Such advanced kinetic experiments are required to untangle the intricate networks of transfer pathways and the factors affecting flux through branch points. High sensitivity and suitability with high-throughput methodology are additional benefits of this approach. We anticipate that this cluster detection methodology will transform the study of Fe-S cluster pathways and potentially other metal cofactor biosynthetic pathways. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25478817</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5126</ISSN><JournalIssue CitedMedium="Internet"><Volume>137</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Jan</Month><Day>14</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J Am Chem Soc</ISOAbbreviation></Journal><ArticleTitle>Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.</ArticleTitle><Pagination><MedlinePgn>390-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/ja510998s</ELocationID><Abstract><AbstractText>Iron-sulfur (Fe-S) clusters are protein cofactors that are constructed and delivered to target proteins by elaborate biosynthetic machinery. Mechanistic insights into these processes have been limited by the lack of sensitive probes for tracking Fe-S cluster synthesis and transfer reactions. Here we present fusion protein- and intein-based fluorescent labeling strategies that can probe Fe-S cluster binding. The fluorescence is sensitive to different cluster types ([2Fe-2S] and [4Fe-4S] clusters), ligand environments ([2Fe-2S] clusters on Rieske, ferredoxin (Fdx), and glutaredoxin), and cluster oxidation states. The power of this approach is highlighted with an extreme example in which the kinetics of Fe-S cluster transfer reactions are monitored between two Fdx molecules that have identical Fe-S spectroscopic properties. This exchange reaction between labeled and unlabeled Fdx is catalyzed by dithiothreitol (DTT), a result that was confirmed by mass spectrometry. DTT likely functions in a ligand substitution reaction that generates a [2Fe-2S]-DTT species, which can transfer the cluster to either labeled or unlabeled Fdx. The ability to monitor this challenging cluster exchange reaction indicates that real-time Fe-S cluster incorporation can be tracked for a specific labeled protein in multicomponent assays that include several unlabeled Fe-S binding proteins or other chromophores. Such advanced kinetic experiments are required to untangle the intricate networks of transfer pathways and the factors affecting flux through branch points. High sensitivity and suitability with high-throughput methodology are additional benefits of this approach. We anticipate that this cluster detection methodology will transform the study of Fe-S cluster pathways and potentially other metal cofactor biosynthetic pathways. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vranish</LastName><ForeName>James N</ForeName><Initials>JN</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics and ‡Department of Chemistry, Texas A&M University , College Station, Texas 77842-3012, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Russell</LastName><ForeName>William K</ForeName><Initials>WK</Initials></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Lusa E</ForeName><Initials>LE</Initials></Author><Author ValidYN="Y"><LastName>Cox</LastName><ForeName>Rachael M</ForeName><Initials>RM</Initials></Author><Author ValidYN="Y"><LastName>Russell</LastName><ForeName>David H</ForeName><Initials>DH</Initials></Author><Author 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Barondeau</name><name sortKey="Cox, Rachael M" sort="Cox, Rachael M" uniqKey="Cox R" first="Rachael M" last="Cox">Rachael M. Cox</name><name sortKey="Russell, David H" sort="Russell, David H" uniqKey="Russell D" first="David H" last="Russell">David H. Russell</name><name sortKey="Russell, William K" sort="Russell, William K" uniqKey="Russell W" first="William K" last="Russell">William K. Russell</name><name sortKey="Yu, Lusa E" sort="Yu, Lusa E" uniqKey="Yu L" first="Lusa E" last="Yu">Lusa E. Yu</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Vranish, James N" sort="Vranish, James N" uniqKey="Vranish J" first="James N" last="Vranish">James N. Vranish</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:25478817
|texte= Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:25478817" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |