drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.
Identifieur interne : 000196 ( Main/Exploration ); précédent : 000195; suivant : 000197drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.
Auteurs : Subhash C. Bihani [Inde] ; Lata Panicker [Inde] ; Yogendra S. Rajpurohit [Inde] ; Hari S. Misra [Inde] ; Vinay Kumar [Inde]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2018.
Descripteurs français
- KwdFr :
- Cristallographie aux rayons X (MeSH), Cytoplasme (composition chimique), Cytoplasme (enzymologie), Deinococcus (composition chimique), Deinococcus (enzymologie), Domaine catalytique (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Motifs d'acides aminés (génétique), Oxydoréduction (MeSH), Protein-disulfide reductase (glutathione) (composition chimique), Protein-disulfide reductase (glutathione) (génétique), Protein-disulfide reductase (glutathione) (métabolisme), Stress oxydatif (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Cytoplasme, Deinococcus, Glutarédoxines, Protein-disulfide reductase (glutathione), Thiorédoxines.
- enzymologie : Cytoplasme, Deinococcus.
- génétique : Glutarédoxines, Motifs d'acides aminés, Protein-disulfide reductase (glutathione), Thiorédoxines.
- métabolisme : Glutarédoxines, Protein-disulfide reductase (glutathione), Thiorédoxines.
- Cristallographie aux rayons X, Domaine catalytique, Oxydoréduction, Stress oxydatif.
English descriptors
- KwdEn :
- Amino Acid Motifs (genetics), Catalytic Domain (MeSH), Crystallography, X-Ray (MeSH), Cytoplasm (chemistry), Cytoplasm (enzymology), Deinococcus (chemistry), Deinococcus (enzymology), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Protein Disulfide Reductase (Glutathione) (chemistry), Protein Disulfide Reductase (Glutathione) (genetics), Protein Disulfide Reductase (Glutathione) (metabolism), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Protein Disulfide Reductase (Glutathione), Thioredoxins.
- chemistry : Cytoplasm, Deinococcus.
- enzymology : Cytoplasm, Deinococcus.
- genetics : Amino Acid Motifs, Glutaredoxins, Protein Disulfide Reductase (Glutathione), Thioredoxins.
- chemical , metabolism : Glutaredoxins, Protein Disulfide Reductase (Glutathione), Thioredoxins.
- Catalytic Domain, Crystallography, X-Ray, Oxidation-Reduction, Oxidative Stress.
Abstract
AIMS
Living cells employ thioredoxin and glutaredoxin disulfide oxido-reductases to protect thiol groups in intracellular proteins. FrnE protein of Deinococcus radiodurans (drFrnE) is a disulfide oxido-reductase that is induced in response to Cd
RESULTS
Here, we show drFrnE as a novel cytoplasmic oxido-reductase that could be functional in eubacteria under conditions where thioredoxin/glutaredoxin systems are inhibited or absent. Crystal structure analysis of drFrnE reveals thioredoxin fold with an alpha helical insertion domain and a unique, flexible, and functionally important C-terminal tail. The C-tail harbors a novel 239-CX
DOI: 10.1089/ars.2016.6960
PubMed: 28899103
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Bihani</name><affiliation wicri:level="1"><nlm:affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation></author><author><name sortKey="Panicker, Lata" sort="Panicker, Lata" uniqKey="Panicker L" first="Lata" last="Panicker">Lata Panicker</name><affiliation wicri:level="1"><nlm:affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation></author><author><name sortKey="Rajpurohit, Yogendra S" sort="Rajpurohit, Yogendra S" uniqKey="Rajpurohit Y" first="Yogendra S" last="Rajpurohit">Yogendra S. Rajpurohit</name><affiliation wicri:level="1"><nlm:affiliation>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation></author><author><name sortKey="Misra, Hari S" sort="Misra, Hari S" uniqKey="Misra H" first="Hari S" last="Misra">Hari S. Misra</name><affiliation wicri:level="1"><nlm:affiliation>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>3 Life Sciences, Homi Bhabha National Institute , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>3 Life Sciences, Homi Bhabha National Institute , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation></author><author><name sortKey="Kumar, Vinay" sort="Kumar, Vinay" uniqKey="Kumar V" first="Vinay" last="Kumar">Vinay Kumar</name><affiliation wicri:level="1"><nlm:affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>3 Life Sciences, Homi Bhabha National Institute , Mumbai, India .</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>3 Life Sciences, Homi Bhabha National Institute , Mumbai</wicri:regionArea><wicri:noRegion>Mumbai</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (genetics)</term><term>Catalytic Domain (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cytoplasm (chemistry)</term><term>Cytoplasm (enzymology)</term><term>Deinococcus (chemistry)</term><term>Deinococcus (enzymology)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (chemistry)</term><term>Protein Disulfide Reductase (Glutathione) (genetics)</term><term>Protein Disulfide Reductase (Glutathione) (metabolism)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X (MeSH)</term><term>Cytoplasme (composition chimique)</term><term>Cytoplasme (enzymologie)</term><term>Deinococcus (composition chimique)</term><term>Deinococcus (enzymologie)</term><term>Domaine catalytique (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Motifs d'acides aminés (génétique)</term><term>Oxydoréduction (MeSH)</term><term>Protein-disulfide reductase (glutathione) (composition chimique)</term><term>Protein-disulfide reductase (glutathione) (génétique)</term><term>Protein-disulfide reductase (glutathione) (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytoplasm</term><term>Deinococcus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cytoplasme</term><term>Deinococcus</term><term>Glutarédoxines</term><term>Protein-disulfide reductase (glutathione)</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cytoplasme</term><term>Deinococcus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cytoplasm</term><term>Deinococcus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Motifs d'acides aminés</term><term>Protein-disulfide reductase (glutathione)</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Protein-disulfide reductase (glutathione)</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallographie aux rayons X</term><term>Domaine catalytique</term><term>Oxydoréduction</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Living cells employ thioredoxin and glutaredoxin disulfide oxido-reductases to protect thiol groups in intracellular proteins. FrnE protein of Deinococcus radiodurans (drFrnE) is a disulfide oxido-reductase that is induced in response to Cd</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Here, we show drFrnE as a novel cytoplasmic oxido-reductase that could be functional in eubacteria under conditions where thioredoxin/glutaredoxin systems are inhibited or absent. Crystal structure analysis of drFrnE reveals thioredoxin fold with an alpha helical insertion domain and a unique, flexible, and functionally important C-terminal tail. The C-tail harbors a novel 239-CX</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28899103</PMID><DateCompleted><Year>2018</Year><Month>08</Month><Day>31</Day></DateCompleted><DateRevised><Year>2018</Year><Month>08</Month><Day>31</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>4</Issue><PubDate><Year>2018</Year><Month>02</Month><Day>01</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.</ArticleTitle><Pagination><MedlinePgn>296-310</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2016.6960</ELocationID><Abstract><AbstractText Label="AIMS">Living cells employ thioredoxin and glutaredoxin disulfide oxido-reductases to protect thiol groups in intracellular proteins. FrnE protein of Deinococcus radiodurans (drFrnE) is a disulfide oxido-reductase that is induced in response to Cd<sup>2+</sup> exposure and is involved in cadmium and radiation tolerance. The aim of this study is to probe structure, function, and cellular localization of FrnE class of proteins.</AbstractText><AbstractText Label="RESULTS">Here, we show drFrnE as a novel cytoplasmic oxido-reductase that could be functional in eubacteria under conditions where thioredoxin/glutaredoxin systems are inhibited or absent. Crystal structure analysis of drFrnE reveals thioredoxin fold with an alpha helical insertion domain and a unique, flexible, and functionally important C-terminal tail. The C-tail harbors a novel 239-CX<sub>4</sub>C-244 motif that interacts with the active site 22-CXXC-25 motif. Crystal structures with different active site redox states, including mixed disulfide (Cys22-Cys244), are reported here. The biochemical data show that 239-CX<sub>4</sub>C-244 motif channels electrons to the active site cysteines. drFrnE is more stable in the oxidized form, compared with the reduced form, supporting its role as a disulfide reductase. Using bioinformatics analysis and fluorescence microscopy, we show cytoplasmic localization of drFrnE. We have found "true" orthologs of drFrnE in several eubacterial phyla and, interestingly, all these groups apparently lack a functional glutaredoxin system. Innovation and Conclusion: We show that drFrnE represents a new class of hitherto unknown intracellular oxido-reductases that are abundantly present in eubacteria. Unlike other well-known oxido-reductases, FrnE harbors an additional dithiol motif that acts as a conduit to channel electrons to the active site during catalytic turnover. Antioxid. Redox Signal. 28, 296-310.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bihani</LastName><ForeName>Subhash C</ForeName><Initials>SC</Initials><AffiliationInfo><Affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Panicker</LastName><ForeName>Lata</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rajpurohit</LastName><ForeName>Yogendra S</ForeName><Initials>YS</Initials><AffiliationInfo><Affiliation>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai, India .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Misra</LastName><ForeName>Hari S</ForeName><Initials>HS</Initials><AffiliationInfo><Affiliation>2 Molecular Biology Division, Bhabha Atomic Research Centre , Mumbai, India .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>3 Life Sciences, Homi Bhabha National Institute , Mumbai, India .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Vinay</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>1 Protein Crystallography Section, Radiation Biology & Health Sciences Division, Bhabha Atomic Research Centre , Mumbai, India .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>3 Life Sciences, Homi Bhabha National Institute , Mumbai, India .</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>10</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D034301" MajorTopicYN="N">Deinococcus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Deinococcus</Keyword><Keyword MajorTopicYN="Y">FrnE</Keyword><Keyword MajorTopicYN="Y">cytoplasmic disulfide oxido-reductase</Keyword><Keyword MajorTopicYN="Y">disulfide reductase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>9</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28899103</ArticleId><ArticleId IdType="doi">10.1089/ars.2016.6960</ArticleId><ArticleId IdType="pii">10.1089/ars.2016.6960</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Bihani, Subhash C" sort="Bihani, Subhash C" uniqKey="Bihani S" first="Subhash C" last="Bihani">Subhash C. Bihani</name></noRegion><name sortKey="Kumar, Vinay" sort="Kumar, Vinay" uniqKey="Kumar V" first="Vinay" last="Kumar">Vinay Kumar</name><name sortKey="Kumar, Vinay" sort="Kumar, Vinay" uniqKey="Kumar V" first="Vinay" last="Kumar">Vinay Kumar</name><name sortKey="Misra, Hari S" sort="Misra, Hari S" uniqKey="Misra H" first="Hari S" last="Misra">Hari S. Misra</name><name sortKey="Misra, Hari S" sort="Misra, Hari S" uniqKey="Misra H" first="Hari S" last="Misra">Hari S. Misra</name><name sortKey="Panicker, Lata" sort="Panicker, Lata" uniqKey="Panicker L" first="Lata" last="Panicker">Lata Panicker</name><name sortKey="Rajpurohit, Yogendra S" sort="Rajpurohit, Yogendra S" uniqKey="Rajpurohit Y" first="Yogendra S" last="Rajpurohit">Yogendra S. Rajpurohit</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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