Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.
Identifieur interne : 000119 ( Main/Exploration ); précédent : 000118; suivant : 000120Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.
Auteurs : Manuela Gellert [Allemagne] ; Md Faruq Hossain [Allemagne] ; Felix Jacob Ferdinand Berens [Allemagne] ; Lukas Willy Bruhn [Allemagne] ; Claudia Urbainsky [Allemagne] ; Volkmar Liebscher [Allemagne] ; Christopher Horst Lillig [Allemagne]Source :
- Heliyon [ 2405-8440 ] ; 2019.
Abstract
The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyze thiol-disulfide exchange reactions and the proteins are widely recognized for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity - a prerequisite for redox switching. Despite of multiple efforts, the true nature for this specificity is still under debate. Here, we comprehensively compare the classification/clustering of various redoxins from all domains of life based on their similarity in amino acid sequence, tertiary structure, and their electrostatic properties. We correlate these similarities to the existence of common interaction partners, identified in various previous studies and suggested by proteomic screenings. These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases. Instead, a number of examples clearly demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies.
DOI: 10.1016/j.heliyon.2019.e02943
PubMed: 31890941
PubMed Central: PMC6928294
Affiliations:
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Greifswald</wicri:regionArea><wicri:noRegion>University Medicine Greifswald</wicri:noRegion><wicri:noRegion>University Medicine Greifswald</wicri:noRegion><wicri:noRegion>University Medicine Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Liebscher, Volkmar" sort="Liebscher, Volkmar" uniqKey="Liebscher V" first="Volkmar" last="Liebscher">Volkmar Liebscher</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Mathematics and Informatics, University of Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Mathematics and Informatics, University of Greifswald</wicri:regionArea><wicri:noRegion>University of Greifswald</wicri:noRegion><wicri:noRegion>University of Greifswald</wicri:noRegion><wicri:noRegion>University of Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald</wicri:regionArea><wicri:noRegion>University Medicine Greifswald</wicri:noRegion><wicri:noRegion>University Medicine Greifswald</wicri:noRegion><wicri:noRegion>University Medicine Greifswald</wicri:noRegion></affiliation></author></analytic><series><title level="j">Heliyon</title><idno type="ISSN">2405-8440</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyze thiol-disulfide exchange reactions and the proteins are widely recognized for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity - a prerequisite for redox switching. Despite of multiple efforts, the true nature for this specificity is still under debate. Here, we comprehensively compare the classification/clustering of various redoxins from all domains of life based on their similarity in amino acid sequence, tertiary structure, and their electrostatic properties. We correlate these similarities to the existence of common interaction partners, identified in various previous studies and suggested by proteomic screenings. These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases. Instead, a number of examples clearly demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">31890941</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2405-8440</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><Issue>12</Issue><PubDate><Year>2019</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Heliyon</Title><ISOAbbreviation>Heliyon</ISOAbbreviation></Journal><ArticleTitle>Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.</ArticleTitle><Pagination><MedlinePgn>e02943</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.heliyon.2019.e02943</ELocationID><Abstract><AbstractText>The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyze thiol-disulfide exchange reactions and the proteins are widely recognized for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity - a prerequisite for redox switching. Despite of multiple efforts, the true nature for this specificity is still under debate. Here, we comprehensively compare the classification/clustering of various redoxins from all domains of life based on their similarity in amino acid sequence, tertiary structure, and their electrostatic properties. We correlate these similarities to the existence of common interaction partners, identified in various previous studies and suggested by proteomic screenings. These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases. Instead, a number of examples clearly demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies.</AbstractText><CopyrightInformation>© 2019 The Author(s).</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gellert</LastName><ForeName>Manuela</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hossain</LastName><ForeName>Md Faruq</ForeName><Initials>MF</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berens</LastName><ForeName>Felix Jacob Ferdinand</ForeName><Initials>FJF</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institute for Mathematics and Informatics, University of Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bruhn</LastName><ForeName>Lukas Willy</ForeName><Initials>LW</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institute for Mathematics and Informatics, University of Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Urbainsky</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liebscher</LastName><ForeName>Volkmar</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Institute for Mathematics and Informatics, University of Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>12</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Heliyon</MedlineTA><NlmUniqueID>101672560</NlmUniqueID><ISSNLinking>2405-8440</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Biocomputational method</Keyword><Keyword MajorTopicYN="N">Biomolecules</Keyword><Keyword MajorTopicYN="N">Electrostatics</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Gromov-Wasserstein distance</Keyword><Keyword MajorTopicYN="N">Mathematical biosciences</Keyword><Keyword MajorTopicYN="N">Molecular docking</Keyword><Keyword MajorTopicYN="N">Protein-protein interaction</Keyword><Keyword MajorTopicYN="N">Redox signaling</Keyword><Keyword MajorTopicYN="N">Thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>05</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>11</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate 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uniqKey="Berens F" first="Felix Jacob Ferdinand" last="Berens">Felix Jacob Ferdinand Berens</name><name sortKey="Bruhn, Lukas Willy" sort="Bruhn, Lukas Willy" uniqKey="Bruhn L" first="Lukas Willy" last="Bruhn">Lukas Willy Bruhn</name><name sortKey="Bruhn, Lukas Willy" sort="Bruhn, Lukas Willy" uniqKey="Bruhn L" first="Lukas Willy" last="Bruhn">Lukas Willy Bruhn</name><name sortKey="Hossain, Md Faruq" sort="Hossain, Md Faruq" uniqKey="Hossain M" first="Md Faruq" last="Hossain">Md Faruq Hossain</name><name sortKey="Liebscher, Volkmar" sort="Liebscher, Volkmar" uniqKey="Liebscher V" first="Volkmar" last="Liebscher">Volkmar Liebscher</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Urbainsky, Claudia" sort="Urbainsky, Claudia" uniqKey="Urbainsky C" first="Claudia" last="Urbainsky">Claudia Urbainsky</name></country></tree></affiliations></record>Pour 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