Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.
Identifieur interne : 000922 ( Main/Exploration ); précédent : 000921; suivant : 000923Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.
Auteurs : Morgan Anne Feeney [États-Unis] ; Karthik Veeravalli ; Dana Boyd ; Stéphanie Gon ; Melinda Jo Faulkner ; George Georgiou ; Jonathan BeckwithSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.
Descripteurs français
- KwdFr :
- ADN bactérien (génétique), Acide lipoïque (analogues et dérivés), Acide lipoïque (métabolisme), Amorces ADN (génétique), Cycle citrique (MeSH), Cytoplasme (métabolisme), Dihydrolipoamide dehydrogenase (génétique), Dihydrolipoamide dehydrogenase (métabolisme), Escherichia coli (croissance et développement), Escherichia coli (génétique), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Glutathione reductase (génétique), Glutathione reductase (métabolisme), Gènes bactériens (MeSH), Modèles biologiques (MeSH), Mutation (MeSH), Oxydoréduction (MeSH), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Ribonucleotide reductases (génétique), Ribonucleotide reductases (métabolisme), Suppression génétique (MeSH), Séquence nucléotidique (MeSH), Thioredoxin-disulfide reductase (génétique), Thioredoxin-disulfide reductase (métabolisme), Transport d'électrons (MeSH), Voies et réseaux métaboliques (MeSH).
- MESH :
- analogues et dérivés : Acide lipoïque.
- croissance et développement : Escherichia coli.
- génétique : ADN bactérien, Amorces ADN, Dihydrolipoamide dehydrogenase, Escherichia coli, Glutathione reductase, Protéines Escherichia coli, Ribonucleotide reductases, Thioredoxin-disulfide reductase.
- métabolisme : Acide lipoïque, Cytoplasme, Dihydrolipoamide dehydrogenase, Escherichia coli, Glutathione reductase, Protéines Escherichia coli, Ribonucleotide reductases, Thioredoxin-disulfide reductase.
- Cycle citrique, Glutarédoxines, Gènes bactériens, Modèles biologiques, Mutation, Oxydoréduction, Suppression génétique, Séquence nucléotidique, Transport d'électrons, Voies et réseaux métaboliques.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Citric Acid Cycle (MeSH), Cytoplasm (metabolism), DNA Primers (genetics), DNA, Bacterial (genetics), Dihydrolipoamide Dehydrogenase (genetics), Dihydrolipoamide Dehydrogenase (metabolism), Electron Transport (MeSH), Escherichia coli (genetics), Escherichia coli (growth & development), Escherichia coli (metabolism), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Genes, Bacterial (MeSH), Glutaredoxins (MeSH), Glutathione Reductase (genetics), Glutathione Reductase (metabolism), Metabolic Networks and Pathways (MeSH), Models, Biological (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Ribonucleotide Reductases (genetics), Ribonucleotide Reductases (metabolism), Suppression, Genetic (MeSH), Thioctic Acid (analogs & derivatives), Thioctic Acid (metabolism), Thioredoxin-Disulfide Reductase (genetics), Thioredoxin-Disulfide Reductase (metabolism).
- MESH :
- chemical , analogs & derivatives : Thioctic Acid.
- chemical , genetics : DNA Primers, DNA, Bacterial, Dihydrolipoamide Dehydrogenase, Escherichia coli Proteins, Glutathione Reductase, Ribonucleotide Reductases, Thioredoxin-Disulfide Reductase.
- genetics : Escherichia coli.
- growth & development : Escherichia coli.
- metabolism : Cytoplasm, Dihydrolipoamide Dehydrogenase, Escherichia coli, Escherichia coli Proteins, Glutathione Reductase, Ribonucleotide Reductases, Thioctic Acid, Thioredoxin-Disulfide Reductase.
- Base Sequence, Citric Acid Cycle, Electron Transport, Genes, Bacterial, Glutaredoxins, Metabolic Networks and Pathways, Models, Biological, Mutation, Oxidation-Reduction, Suppression, Genetic.
Abstract
In bacteria, cysteines of cytoplasmic proteins, including the essential enzyme ribonucleotide reductase (RNR), are maintained in the reduced state by the thioredoxin and glutathione/glutaredoxin pathways. An Escherichia coli mutant lacking both glutathione reductase and thioredoxin reductase cannot grow because RNR is disulfide bonded and nonfunctional. Here we report that suppressor mutations in the lpdA gene, which encodes the oxidative enzyme lipoamide dehydrogenase required for tricarboxylic acid (TCA) cycle functioning, restore growth to this redox-defective mutant. The suppressor mutations reduce LpdA activity, causing the accumulation of dihydrolipoamide, the reduced protein-bound form of lipoic acid. Dihydrolipoamide can then provide electrons for the reactivation of RNR through reduction of glutaredoxins. Dihydrolipoamide is oxidized in the process, restoring function to the TCA cycle. Thus, two electron transfer pathways are rewired to meet both oxidative and reductive needs of the cell: dihydrolipoamide functionally replaces glutathione, and the glutaredoxins replace LpdA. Both lipoic acid and glutaredoxins act in the reverse manner from their normal cellular functions. Bioinformatic analysis suggests that such activities may also function in other bacteria.
DOI: 10.1073/pnas.1105429108
PubMed: 21521794
PubMed Central: PMC3093452
Affiliations:
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level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Citric Acid Cycle (MeSH)</term><term>Cytoplasm (metabolism)</term><term>DNA Primers (genetics)</term><term>DNA, Bacterial (genetics)</term><term>Dihydrolipoamide Dehydrogenase (genetics)</term><term>Dihydrolipoamide Dehydrogenase (metabolism)</term><term>Electron Transport (MeSH)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (growth & development)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (genetics)</term><term>Escherichia coli Proteins (metabolism)</term><term>Genes, Bacterial (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione Reductase (genetics)</term><term>Glutathione Reductase (metabolism)</term><term>Metabolic Networks and Pathways (MeSH)</term><term>Models, Biological (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Ribonucleotide Reductases (genetics)</term><term>Ribonucleotide Reductases (metabolism)</term><term>Suppression, Genetic (MeSH)</term><term>Thioctic Acid (analogs & derivatives)</term><term>Thioctic Acid (metabolism)</term><term>Thioredoxin-Disulfide Reductase (genetics)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (génétique)</term><term>Acide lipoïque (analogues et dérivés)</term><term>Acide lipoïque (métabolisme)</term><term>Amorces ADN (génétique)</term><term>Cycle citrique (MeSH)</term><term>Cytoplasme (métabolisme)</term><term>Dihydrolipoamide dehydrogenase (génétique)</term><term>Dihydrolipoamide dehydrogenase (métabolisme)</term><term>Escherichia coli (croissance et développement)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Glutathione reductase (génétique)</term><term>Glutathione reductase (métabolisme)</term><term>Gènes bactériens (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Mutation (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines Escherichia coli (génétique)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Ribonucleotide reductases (génétique)</term><term>Ribonucleotide reductases (métabolisme)</term><term>Suppression génétique (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Thioredoxin-disulfide reductase (génétique)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Transport d'électrons (MeSH)</term><term>Voies et réseaux métaboliques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Thioctic Acid</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>DNA, Bacterial</term><term>Dihydrolipoamide Dehydrogenase</term><term>Escherichia coli Proteins</term><term>Glutathione Reductase</term><term>Ribonucleotide Reductases</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Acide lipoïque</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN bactérien</term><term>Amorces ADN</term><term>Dihydrolipoamide dehydrogenase</term><term>Escherichia coli</term><term>Glutathione reductase</term><term>Protéines Escherichia coli</term><term>Ribonucleotide reductases</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term><term>Dihydrolipoamide Dehydrogenase</term><term>Escherichia coli</term><term>Escherichia coli Proteins</term><term>Glutathione Reductase</term><term>Ribonucleotide Reductases</term><term>Thioctic Acid</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide lipoïque</term><term>Cytoplasme</term><term>Dihydrolipoamide dehydrogenase</term><term>Escherichia coli</term><term>Glutathione reductase</term><term>Protéines Escherichia coli</term><term>Ribonucleotide reductases</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Citric Acid Cycle</term><term>Electron Transport</term><term>Genes, Bacterial</term><term>Glutaredoxins</term><term>Metabolic Networks and Pathways</term><term>Models, Biological</term><term>Mutation</term><term>Oxidation-Reduction</term><term>Suppression, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cycle citrique</term><term>Glutarédoxines</term><term>Gènes bactériens</term><term>Modèles biologiques</term><term>Mutation</term><term>Oxydoréduction</term><term>Suppression génétique</term><term>Séquence nucléotidique</term><term>Transport d'électrons</term><term>Voies et réseaux métaboliques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In bacteria, cysteines of cytoplasmic proteins, including the essential enzyme ribonucleotide reductase (RNR), are maintained in the reduced state by the thioredoxin and glutathione/glutaredoxin pathways. An Escherichia coli mutant lacking both glutathione reductase and thioredoxin reductase cannot grow because RNR is disulfide bonded and nonfunctional. Here we report that suppressor mutations in the lpdA gene, which encodes the oxidative enzyme lipoamide dehydrogenase required for tricarboxylic acid (TCA) cycle functioning, restore growth to this redox-defective mutant. The suppressor mutations reduce LpdA activity, causing the accumulation of dihydrolipoamide, the reduced protein-bound form of lipoic acid. Dihydrolipoamide can then provide electrons for the reactivation of RNR through reduction of glutaredoxins. Dihydrolipoamide is oxidized in the process, restoring function to the TCA cycle. Thus, two electron transfer pathways are rewired to meet both oxidative and reductive needs of the cell: dihydrolipoamide functionally replaces glutathione, and the glutaredoxins replace LpdA. Both lipoic acid and glutaredoxins act in the reverse manner from their normal cellular functions. Bioinformatic analysis suggests that such activities may also function in other bacteria.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21521794</PMID><DateCompleted><Year>2011</Year><Month>07</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>108</Volume><Issue>19</Issue><PubDate><Year>2011</Year><Month>May</Month><Day>10</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>7991-6</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1105429108</ELocationID><Abstract><AbstractText>In bacteria, cysteines of cytoplasmic proteins, including the essential enzyme ribonucleotide reductase (RNR), are maintained in the reduced state by the thioredoxin and glutathione/glutaredoxin pathways. An Escherichia coli mutant lacking both glutathione reductase and thioredoxin reductase cannot grow because RNR is disulfide bonded and nonfunctional. Here we report that suppressor mutations in the lpdA gene, which encodes the oxidative enzyme lipoamide dehydrogenase required for tricarboxylic acid (TCA) cycle functioning, restore growth to this redox-defective mutant. The suppressor mutations reduce LpdA activity, causing the accumulation of dihydrolipoamide, the reduced protein-bound form of lipoic acid. Dihydrolipoamide can then provide electrons for the reactivation of RNR through reduction of glutaredoxins. Dihydrolipoamide is oxidized in the process, restoring function to the TCA cycle. Thus, two electron transfer pathways are rewired to meet both oxidative and reductive needs of the cell: dihydrolipoamide functionally replaces glutathione, and the glutaredoxins replace LpdA. Both lipoic acid and glutaredoxins act in the reverse manner from their normal cellular functions. Bioinformatic analysis suggests that such activities may also function in other bacteria.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Feeney</LastName><ForeName>Morgan Anne</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Veeravalli</LastName><ForeName>Karthik</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Boyd</LastName><ForeName>Dana</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Gon</LastName><ForeName>Stéphanie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Faulkner</LastName><ForeName>Melinda Jo</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Georgiou</LastName><ForeName>George</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Beckwith</LastName><ForeName>Jonathan</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM041883</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM055090</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM41883</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM55090</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>04</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004269">DNA, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3884-47-7</RegistryNumber><NameOfSubstance UI="C007409">dihydrolipoamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>73Y7P0K73Y</RegistryNumber><NameOfSubstance UI="D008063">Thioctic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.-</RegistryNumber><NameOfSubstance UI="D012264">Ribonucleotide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.4</RegistryNumber><NameOfSubstance UI="D008058">Dihydrolipoamide Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002952" MajorTopicYN="N">Citric Acid Cycle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004269" MajorTopicYN="N">DNA, Bacterial</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008058" MajorTopicYN="N">Dihydrolipoamide Dehydrogenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029968" MajorTopicYN="N">Escherichia coli Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005798" MajorTopicYN="N">Genes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005980" MajorTopicYN="N">Glutathione Reductase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053858" MajorTopicYN="N">Metabolic Networks and Pathways</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013489" MajorTopicYN="N">Suppression, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008063" MajorTopicYN="N">Thioctic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide 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first="Stéphanie" last="Gon">Stéphanie Gon</name><name sortKey="Veeravalli, Karthik" sort="Veeravalli, Karthik" uniqKey="Veeravalli K" first="Karthik" last="Veeravalli">Karthik Veeravalli</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Feeney, Morgan Anne" sort="Feeney, Morgan Anne" uniqKey="Feeney M" first="Morgan Anne" last="Feeney">Morgan Anne Feeney</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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