Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.
Identifieur interne : 001145 ( Main/Exploration ); précédent : 001144; suivant : 001146Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.
Auteurs : E J Stewart [États-Unis] ; F. Aslund ; J. BeckwithSource :
- The EMBO journal [ 0261-4189 ] ; 1998.
Descripteurs français
- KwdFr :
- Compartimentation cellulaire (MeSH), Cytoplasme (métabolisme), Disulfures (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Gènes bactériens (MeSH), Oxydoréduction (MeSH), Phosphatase alcaline (métabolisme), Protéines Escherichia coli (MeSH), Protéines membranaires (métabolisme), Thioredoxin-disulfide reductase (déficit), Thioredoxin-disulfide reductase (génétique), Thiorédoxines (métabolisme).
- MESH :
- déficit : Thioredoxin-disulfide reductase.
- génétique : Escherichia coli, Thioredoxin-disulfide reductase.
- métabolisme : Cytoplasme, Disulfures, Escherichia coli, Phosphatase alcaline, Protéines membranaires, Thiorédoxines.
- Compartimentation cellulaire, Gènes bactériens, Oxydoréduction, Protéines Escherichia coli.
English descriptors
- KwdEn :
- Alkaline Phosphatase (metabolism), Cell Compartmentation (MeSH), Cytoplasm (metabolism), Disulfides (metabolism), Escherichia coli (genetics), Escherichia coli (metabolism), Escherichia coli Proteins (MeSH), Genes, Bacterial (MeSH), Membrane Proteins (metabolism), Oxidation-Reduction (MeSH), Thioredoxin-Disulfide Reductase (deficiency), Thioredoxin-Disulfide Reductase (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , deficiency : Thioredoxin-Disulfide Reductase.
- chemical , genetics : Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Alkaline Phosphatase, Disulfides, Membrane Proteins, Thioredoxins.
- genetics : Escherichia coli.
- metabolism : Cytoplasm, Escherichia coli.
- Cell Compartmentation, Escherichia coli Proteins, Genes, Bacterial, Oxidation-Reduction.
Abstract
Cytoplasmic proteins do not generally contain structural disulfide bonds, although certain cytoplasmic enzymes form such bonds as part of their catalytic cycles. The disulfide bonds in these latter enzymes are reduced in Escherichia coli by two systems; the thioredoxin pathway and the glutathione/glutaredoxin pathway. However, structural disulfide bonds can form in proteins in the cytoplasm when the gene (trxB) for the enzyme thioredoxin reductase is inactivated by mutation. This disulfide bond formation can be detected by assessing the state of the normally periplasmic enzyme alkaline phosphatase (AP) when it is localized to the cytoplasm. Here we show that the formation of disulfide bonds in cytoplasmic AP in the trxB mutant is dependent on the presence of two thioredoxins in the cell, thioredoxins 1 and 2, the products of the genes trxA and trxC, respectively. Our evidence supports a model in which the oxidized forms of these thioredoxins directly catalyze disulfide bond formation in cytoplasmic AP, a reversal of their normal role. In addition, we show that the recently discovered thioredoxin 2 can perform many of the roles of thioredoxin 1 in vivo, and thus is able to reduce certain essential cytoplasmic enzymes. Our results suggest that the three most effective cytoplasmic disulfide-reducing proteins are thioredoxin 1, thioredoxin 2 and glutaredoxin 1; expression of any one of these is sufficient to support aerobic growth. Our results help to explain how the reducing environment in the cytoplasm is maintained so that disulfide bonds do not normally occur.
DOI: 10.1093/emboj/17.19.5543
PubMed: 9755155
PubMed Central: PMC1170883
Affiliations:
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Beckwith</name></author></analytic><series><title level="j">The EMBO journal</title><idno type="ISSN">0261-4189</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alkaline Phosphatase (metabolism)</term><term>Cell Compartmentation (MeSH)</term><term>Cytoplasm (metabolism)</term><term>Disulfides (metabolism)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (MeSH)</term><term>Genes, Bacterial (MeSH)</term><term>Membrane Proteins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Thioredoxin-Disulfide Reductase (deficiency)</term><term>Thioredoxin-Disulfide Reductase (genetics)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Compartimentation cellulaire (MeSH)</term><term>Cytoplasme (métabolisme)</term><term>Disulfures (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Gènes bactériens (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phosphatase alcaline (métabolisme)</term><term>Protéines Escherichia coli (MeSH)</term><term>Protéines membranaires (métabolisme)</term><term>Thioredoxin-disulfide reductase (déficit)</term><term>Thioredoxin-disulfide reductase (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alkaline Phosphatase</term><term>Disulfides</term><term>Membrane Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytoplasme</term><term>Disulfures</term><term>Escherichia coli</term><term>Phosphatase alcaline</term><term>Protéines membranaires</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Compartmentation</term><term>Escherichia coli Proteins</term><term>Genes, Bacterial</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Compartimentation cellulaire</term><term>Gènes bactériens</term><term>Oxydoréduction</term><term>Protéines Escherichia coli</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cytoplasmic proteins do not generally contain structural disulfide bonds, although certain cytoplasmic enzymes form such bonds as part of their catalytic cycles. The disulfide bonds in these latter enzymes are reduced in Escherichia coli by two systems; the thioredoxin pathway and the glutathione/glutaredoxin pathway. However, structural disulfide bonds can form in proteins in the cytoplasm when the gene (trxB) for the enzyme thioredoxin reductase is inactivated by mutation. This disulfide bond formation can be detected by assessing the state of the normally periplasmic enzyme alkaline phosphatase (AP) when it is localized to the cytoplasm. Here we show that the formation of disulfide bonds in cytoplasmic AP in the trxB mutant is dependent on the presence of two thioredoxins in the cell, thioredoxins 1 and 2, the products of the genes trxA and trxC, respectively. Our evidence supports a model in which the oxidized forms of these thioredoxins directly catalyze disulfide bond formation in cytoplasmic AP, a reversal of their normal role. In addition, we show that the recently discovered thioredoxin 2 can perform many of the roles of thioredoxin 1 in vivo, and thus is able to reduce certain essential cytoplasmic enzymes. Our results suggest that the three most effective cytoplasmic disulfide-reducing proteins are thioredoxin 1, thioredoxin 2 and glutaredoxin 1; expression of any one of these is sufficient to support aerobic growth. Our results help to explain how the reducing environment in the cytoplasm is maintained so that disulfide bonds do not normally occur.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9755155</PMID><DateCompleted><Year>1998</Year><Month>11</Month><Day>23</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>19</Issue><PubDate><Year>1998</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J</ISOAbbreviation></Journal><ArticleTitle>Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.</ArticleTitle><Pagination><MedlinePgn>5543-50</MedlinePgn></Pagination><Abstract><AbstractText>Cytoplasmic proteins do not generally contain structural disulfide bonds, although certain cytoplasmic enzymes form such bonds as part of their catalytic cycles. The disulfide bonds in these latter enzymes are reduced in Escherichia coli by two systems; the thioredoxin pathway and the glutathione/glutaredoxin pathway. However, structural disulfide bonds can form in proteins in the cytoplasm when the gene (trxB) for the enzyme thioredoxin reductase is inactivated by mutation. This disulfide bond formation can be detected by assessing the state of the normally periplasmic enzyme alkaline phosphatase (AP) when it is localized to the cytoplasm. Here we show that the formation of disulfide bonds in cytoplasmic AP in the trxB mutant is dependent on the presence of two thioredoxins in the cell, thioredoxins 1 and 2, the products of the genes trxA and trxC, respectively. Our evidence supports a model in which the oxidized forms of these thioredoxins directly catalyze disulfide bond formation in cytoplasmic AP, a reversal of their normal role. In addition, we show that the recently discovered thioredoxin 2 can perform many of the roles of thioredoxin 1 in vivo, and thus is able to reduce certain essential cytoplasmic enzymes. Our results suggest that the three most effective cytoplasmic disulfide-reducing proteins are thioredoxin 1, thioredoxin 2 and glutaredoxin 1; expression of any one of these is sufficient to support aerobic growth. Our results help to explain how the reducing environment in the cytoplasm is maintained so that disulfide bonds do not normally occur.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stewart</LastName><ForeName>E J</ForeName><Initials>EJ</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Beckwith</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM41883</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research 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Aslund</name><name sortKey="Beckwith, J" sort="Beckwith, J" uniqKey="Beckwith J" first="J" last="Beckwith">J. Beckwith</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Stewart, E J" sort="Stewart, E J" uniqKey="Stewart E" first="E J" last="Stewart">E J Stewart</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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