Molecular mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.
Identifieur interne : 000042 ( Main/Exploration ); précédent : 000041; suivant : 000043Molecular mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.
Auteurs : Xiaona Li ; Yang Liu ; Jingyi Zhong ; Chengchuan Che ; Zhijin Gong ; Meiru Si ; Ge YangSource :
- The Journal of general and applied microbiology [ 1349-8037 ] ; 2020.
Abstract
Glutaredoxins (Grxs) with Cys-Pro-Phe (Tyr)-Cys motif and a thioredoxin fold structure play an important role in the anti-oxidant system of bacteria by catalyzing a variety of thiol-disulfide exchange reactions with a 2-Cys mechanism or a 1-Cys mechanism. However, the catalytic and physiological mechanism of Corynebacterium glutamicum Mycoredoxin 1 (Mrx1) that shares a high amino acid sequence similarity to Grxs has not been fully elucidated. Here, we report that Mrx1 has a protective function against various adverse conditions, and the decrease of cell viability to various stress conditions by deletion of the Mrx1 in C. glutamicum was confirmed in the mrx1 mutant. The physiological roles of Mrx1 in defence to oxidative stress were corroborated by its induced expression under various stresses, regulated directly by the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. As well as reducing mycothiol (MSH) mixed disulfide bonds via a 1-Cys mechanism, C. glutamicum Mrx1 catalytically reduced the disulfides in the Ib RNR, insulin and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) by exclusively linking the MSH/Mtr (mycothiol disulfide reductase)/NADPH electron pathway via a 2-Cys mechanism. Thus, we present the first evidence that the Mrx1 is able to protect against the damaging effects of various exogenous stresses by acting as a disulfide oxidoreductase, thereby giving a new insight in how C. glutamicum survives oxidative stressful conditions.
DOI: 10.2323/jgam.2020.03.002
PubMed: 33148889
Affiliations:
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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="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="Si, Meiru" sort="Si, Meiru" uniqKey="Si M" first="Meiru" last="Si">Meiru Si</name><affiliation><nlm:affiliation>College of Life Sciences, Qufu Normal University.</nlm:affiliation><wicri:noCountry code="subField">Qufu 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mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.</title><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="Liu, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang 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="Zhong, Jingyi" sort="Zhong, Jingyi" uniqKey="Zhong J" first="Jingyi" last="Zhong">Jingyi Zhong</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="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="Si, Meiru" sort="Si, Meiru" uniqKey="Si M" first="Meiru" last="Si">Meiru Si</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) with Cys-Pro-Phe (Tyr)-Cys motif and a thioredoxin fold structure play an important role in the anti-oxidant system of bacteria by catalyzing a variety of thiol-disulfide exchange reactions with a 2-Cys mechanism or a 1-Cys mechanism. However, the catalytic and physiological mechanism of Corynebacterium glutamicum Mycoredoxin 1 (Mrx1) that shares a high amino acid sequence similarity to Grxs has not been fully elucidated. Here, we report that Mrx1 has a protective function against various adverse conditions, and the decrease of cell viability to various stress conditions by deletion of the Mrx1 in C. glutamicum was confirmed in the mrx1 mutant. The physiological roles of Mrx1 in defence to oxidative stress were corroborated by its induced expression under various stresses, regulated directly by the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. As well as reducing mycothiol (MSH) mixed disulfide bonds via a 1-Cys mechanism, C. glutamicum Mrx1 catalytically reduced the disulfides in the Ib RNR, insulin and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) by exclusively linking the MSH/Mtr (mycothiol disulfide reductase)/NADPH electron pathway via a 2-Cys mechanism. Thus, we present the first evidence that the Mrx1 is able to protect against the damaging effects of various exogenous stresses by acting as a disulfide oxidoreductase, thereby giving a new insight in how C. glutamicum survives oxidative stressful conditions.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33148889</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1349-8037</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Nov</Month><Day>04</Day></PubDate></JournalIssue><Title>The Journal of general and applied microbiology</Title><ISOAbbreviation>J Gen Appl Microbiol</ISOAbbreviation></Journal><ArticleTitle>Molecular mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.2323/jgam.2020.03.002</ELocationID><Abstract><AbstractText>Glutaredoxins (Grxs) with Cys-Pro-Phe (Tyr)-Cys motif and a thioredoxin fold structure play an important role in the anti-oxidant system of bacteria by catalyzing a variety of thiol-disulfide exchange reactions with a 2-Cys mechanism or a 1-Cys mechanism. However, the catalytic and physiological mechanism of Corynebacterium glutamicum Mycoredoxin 1 (Mrx1) that shares a high amino acid sequence similarity to Grxs has not been fully elucidated. Here, we report that Mrx1 has a protective function against various adverse conditions, and the decrease of cell viability to various stress conditions by deletion of the Mrx1 in C. glutamicum was confirmed in the mrx1 mutant. The physiological roles of Mrx1 in defence to oxidative stress were corroborated by its induced expression under various stresses, regulated directly by the stress-responsive extracytoplasmic function-sigma (ECF-σ) factor SigH. As well as reducing mycothiol (MSH) mixed disulfide bonds via a 1-Cys mechanism, C. glutamicum Mrx1 catalytically reduced the disulfides in the Ib RNR, insulin and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) by exclusively linking the MSH/Mtr (mycothiol disulfide reductase)/NADPH electron pathway via a 2-Cys mechanism. Thus, we present the first evidence that the Mrx1 is able to protect against the damaging effects of various exogenous stresses by acting as a disulfide oxidoreductase, thereby giving a new insight in how C. glutamicum survives oxidative stressful conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><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>Liu</LastName><ForeName>Yang</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhong</LastName><ForeName>Jingyi</ForeName><Initials>J</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>Gong</LastName><ForeName>Zhijin</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>College of Life Sciences, Qufu Normal University.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Si</LastName><ForeName>Meiru</ForeName><Initials>M</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>11</Month><Day>04</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">Corynebacterium glutamicum</Keyword><Keyword MajorTopicYN="N">Mycoredoxin-1</Keyword><Keyword MajorTopicYN="N">mycothiol</Keyword><Keyword MajorTopicYN="N">oxidative stress</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>11</Month><Day>5</Day><Hour>5</Hour><Minute>58</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>11</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33148889</ArticleId><ArticleId IdType="doi">10.2323/jgam.2020.03.002</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, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang Liu</name><name sortKey="Si, Meiru" sort="Si, Meiru" uniqKey="Si M" first="Meiru" last="Si">Meiru Si</name><name sortKey="Yang, Ge" sort="Yang, Ge" uniqKey="Yang G" first="Ge" last="Yang">Ge Yang</name><name sortKey="Zhong, Jingyi" sort="Zhong, Jingyi" uniqKey="Zhong J" first="Jingyi" last="Zhong">Jingyi Zhong</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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