Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses and displays thioredoxin-like activity.
Identifieur interne : 000082 ( Main/Exploration ); précédent : 000081; suivant : 000083Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses and displays thioredoxin-like activity.
Auteurs : Tao Su ; Chengchuan Che ; Ping Sun ; Xiaona Li ; Zhijin Gong ; Jinfeng Liu ; Ge YangSource :
- The Journal of general and applied microbiology [ 1349-8037 ] ; 2020.
Abstract
Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in ribonucleotide reductase (RNR), insulin and 5,5'-dithiobis-(2-nitro-benzoicacid) (DTNB), but also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 were necessary to maintain its activity. The mrx3 deletion mutant showed decreased resistance to various stress, and these sensitive phenotypes were almost fully restored in the complementary strain. The physiological roles of Mrx3 in resistance to various stress were further supported by the induced expression of mrx3 under various stress conditions, directly under the control of the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. Thus, we presented the first evidence that Mrx3 protected against various oxidative stresses by acting as a disulfide oxidoreductase behaving like Trx.
DOI: 10.2323/jgam.2019.10.003
PubMed: 33132239
Affiliations:
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University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Li, Xiaona" sort="Li, Xiaona" uniqKey="Li X" first="Xiaona" last="Li">Xiaona Li</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Gong, Zhijin" sort="Gong, Zhijin" uniqKey="Gong Z" first="Zhijin" last="Gong">Zhijin Gong</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Liu, Jinfeng" sort="Liu, Jinfeng" uniqKey="Liu J" first="Jinfeng" last="Liu">Jinfeng Liu</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Yang, Ge" sort="Yang, Ge" uniqKey="Yang G" first="Ge" last="Yang">Ge Yang</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:33132239</idno><idno type="pmid">33132239</idno><idno type="doi">10.2323/jgam.2019.10.003</idno><idno type="wicri:Area/Main/Corpus">000004</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000004</idno><idno type="wicri:Area/Main/Curation">000004</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000004</idno><idno type="wicri:Area/Main/Exploration">000004</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses and displays thioredoxin-like activity.</title><author><name sortKey="Su, Tao" sort="Su, Tao" uniqKey="Su T" first="Tao" last="Su">Tao Su</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Che, Chengchuan" sort="Che, Chengchuan" uniqKey="Che C" first="Chengchuan" last="Che">Chengchuan Che</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Sun, Ping" sort="Sun, Ping" uniqKey="Sun P" first="Ping" last="Sun">Ping Sun</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Li, Xiaona" sort="Li, Xiaona" uniqKey="Li X" first="Xiaona" last="Li">Xiaona Li</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Gong, Zhijin" sort="Gong, Zhijin" uniqKey="Gong Z" first="Zhijin" last="Gong">Zhijin Gong</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Liu, Jinfeng" sort="Liu, Jinfeng" uniqKey="Liu J" first="Jinfeng" last="Liu">Jinfeng Liu</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author><author><name sortKey="Yang, Ge" sort="Yang, Ge" uniqKey="Yang G" first="Ge" last="Yang">Ge Yang</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu Normal University</wicri:noCountry></affiliation></author></analytic><series><title level="j">The Journal of general and applied microbiology</title><idno type="eISSN">1349-8037</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in ribonucleotide reductase (RNR), insulin and 5,5'-dithiobis-(2-nitro-benzoicacid) (DTNB), but also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 were necessary to maintain its activity. The mrx3 deletion mutant showed decreased resistance to various stress, and these sensitive phenotypes were almost fully restored in the complementary strain. The physiological roles of Mrx3 in resistance to various stress were further supported by the induced expression of mrx3 under various stress conditions, directly under the control of the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. Thus, we presented the first evidence that Mrx3 protected against various oxidative stresses by acting as a disulfide oxidoreductase behaving like Trx.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33132239</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1349-8037</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>30</Day></PubDate></JournalIssue><Title>The Journal of general and applied microbiology</Title><ISOAbbreviation>J Gen Appl Microbiol</ISOAbbreviation></Journal><ArticleTitle>Corynebacterium glutamicum Mycoredoxin 3 protects against multiple oxidative stresses and displays thioredoxin-like activity.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.2323/jgam.2019.10.003</ELocationID><Abstract><AbstractText>Glutaredoxins (Grxs) and thioredoxins (Trxs) play a critical role in resistance to oxidative conditions. However, physiological and biochemical roles of Mycoredoxin 3 (Mrx3) that shared a high amino acid sequence similarity to Grxs remain unknown in Corynebacterium glutamicum. Here we showed that mrx3 deletion strains of C. glutamicum was involved in the protection against oxidative stress. Recombinant Mrx3 not only catalytically reduced the disulfide bonds in ribonucleotide reductase (RNR), insulin and 5,5'-dithiobis-(2-nitro-benzoicacid) (DTNB), but also reduced the mixed disulphides between mycothiol (MSH) and substrate, which was exclusively linked to the thioredoxin reductase (TrxR) electron transfer pathway by a dithiol mechanism. Site-directed mutagenesis confirmed that the conserved Cys17 and Cys20 in Mrx3 were necessary to maintain its activity. The mrx3 deletion mutant showed decreased resistance to various stress, and these sensitive phenotypes were almost fully restored in the complementary strain. The physiological roles of Mrx3 in resistance to various stress were further supported by the induced expression of mrx3 under various stress conditions, directly under the control of the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. Thus, we presented the first evidence that Mrx3 protected against various oxidative stresses by acting as a disulfide oxidoreductase behaving like Trx.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Su</LastName><ForeName>Tao</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Che</LastName><ForeName>Chengchuan</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ping</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xiaona</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gong</LastName><ForeName>Zhijin</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Jinfeng</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Ge</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Japan</Country><MedlineTA>J Gen Appl Microbiol</MedlineTA><NlmUniqueID>0165543</NlmUniqueID><ISSNLinking>0022-1260</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Mycoredoxin 3</Keyword><Keyword MajorTopicYN="N">enzyme activity</Keyword><Keyword MajorTopicYN="N">glutaredoxin-like proteins</Keyword><Keyword MajorTopicYN="N">redox active disulfide</Keyword><Keyword MajorTopicYN="N">redox regulation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>11</Month><Day>2</Day><Hour>6</Hour><Minute>11</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>11</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33132239</ArticleId><ArticleId IdType="doi">10.2323/jgam.2019.10.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Che, Chengchuan" sort="Che, Chengchuan" uniqKey="Che C" first="Chengchuan" last="Che">Chengchuan Che</name><name sortKey="Gong, Zhijin" sort="Gong, Zhijin" uniqKey="Gong Z" first="Zhijin" last="Gong">Zhijin Gong</name><name sortKey="Li, Xiaona" sort="Li, Xiaona" uniqKey="Li X" first="Xiaona" last="Li">Xiaona Li</name><name sortKey="Liu, Jinfeng" sort="Liu, Jinfeng" uniqKey="Liu J" first="Jinfeng" last="Liu">Jinfeng Liu</name><name sortKey="Su, Tao" sort="Su, Tao" uniqKey="Su T" first="Tao" last="Su">Tao Su</name><name sortKey="Sun, Ping" sort="Sun, Ping" uniqKey="Sun P" first="Ping" last="Sun">Ping Sun</name><name sortKey="Yang, Ge" sort="Yang, Ge" uniqKey="Yang G" first="Ge" last="Yang">Ge Yang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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