Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin.
Identifieur interne : 000536 ( Main/Exploration ); précédent : 000535; suivant : 000537Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin.
Auteurs : Moon-Jung Kim [Corée du Sud] ; Jaeho Jeong [Corée du Sud] ; Jihye Jeong [Corée du Sud] ; Kwang Yeon Hwang [Corée du Sud] ; Kong-Joo Lee [Corée du Sud] ; Hwa-Young Kim [Corée du Sud]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2015.
Descripteurs français
- KwdFr :
- Acides sulféniques (composition chimique), Acides sulféniques (métabolisme), Cinétique (MeSH), Clostridium (composition chimique), Clostridium (enzymologie), Clostridium (métabolisme), Cystéine (analogues et dérivés), Cystéine (composition chimique), Cystéine (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Methionine Sulfoxide Reductases (composition chimique), Methionine Sulfoxide Reductases (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- analogues et dérivés : Cystéine.
- composition chimique : Acides sulféniques, Clostridium, Cystéine, Glutarédoxines, Methionine Sulfoxide Reductases.
- enzymologie : Clostridium.
- métabolisme : Acides sulféniques, Clostridium, Cystéine, Glutarédoxines, Glutathion, Methionine Sulfoxide Reductases.
- Cinétique, Données de séquences moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Clostridium (chemistry), Clostridium (enzymology), Clostridium (metabolism), Cysteine (analogs & derivatives), Cysteine (chemistry), Cysteine (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione (metabolism), Kinetics (MeSH), Methionine Sulfoxide Reductases (chemistry), Methionine Sulfoxide Reductases (metabolism), Molecular Sequence Data (MeSH), Sulfenic Acids (chemistry), Sulfenic Acids (metabolism).
- MESH :
- chemical , analogs & derivatives : Cysteine.
- chemistry : Clostridium, Cysteine, Glutaredoxins, Methionine Sulfoxide Reductases, Sulfenic Acids.
- enzymology : Clostridium.
- metabolism : Clostridium, Cysteine, Glutaredoxins, Glutathione, Methionine Sulfoxide Reductases, Sulfenic Acids.
- Amino Acid Sequence, Kinetics, Molecular Sequence Data.
Abstract
Glutaredoxin (Grx), a major redox regulator, can act as a reductant of methionine sulfoxide reductase A (MsrA). However, the biochemical mechanisms involved in MsrA activity regeneration by Grx remain largely unknown. In this study, we investigated the regeneration mechanism of 1-Cys type Clostridium oremlandii MsrA (cMsrA) lacking a resolving Cys residue in a Grx-dependent assay. Kinetic analysis showed that cMsrA could be reduced by both monothiol and dithiol Grxs as efficiently as by in vitro reductant dithiothreitol. Our data revealed that the catalytic Cys sulfenic acid intermediate is not glutathionylated in the presence of the substrate, and that Grx instead directly formed a complex with cMsrA. Mass spectrometry analysis identified a disulfide bond between the N-terminal catalytic Cys of the active site of Grx and the catalytic Cys of cMsrA. This mixed disulfide bond could be resolved by glutathione. Based on these findings, we propose a model for regeneration of 1-Cys type cMsrA by Grx that involves no glutathionylation on the catalytic Cys of cMsrA. This mechanism contrasts with that of the previously known 1-Cys type MsrB.
DOI: 10.1016/j.bbrc.2015.01.025
PubMed: 25600814
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: kjl@ewha.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750</wicri:regionArea><placeName><settlement type="city">Séoul</settlement><region type="capital">Région capitale de Séoul</region></placeName></affiliation></author><author><name sortKey="Kim, Hwa Young" sort="Kim, Hwa Young" uniqKey="Kim H" first="Hwa-Young" last="Kim">Hwa-Young Kim</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea. Electronic address: hykim@ynu.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717</wicri:regionArea><wicri:noRegion>Daegu 705-717</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Clostridium (chemistry)</term><term>Clostridium (enzymology)</term><term>Clostridium (metabolism)</term><term>Cysteine (analogs & derivatives)</term><term>Cysteine (chemistry)</term><term>Cysteine (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Kinetics (MeSH)</term><term>Methionine Sulfoxide Reductases (chemistry)</term><term>Methionine Sulfoxide Reductases (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Sulfenic Acids (chemistry)</term><term>Sulfenic Acids (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides sulféniques (composition chimique)</term><term>Acides sulféniques (métabolisme)</term><term>Cinétique (MeSH)</term><term>Clostridium (composition chimique)</term><term>Clostridium (enzymologie)</term><term>Clostridium (métabolisme)</term><term>Cystéine (analogues et dérivés)</term><term>Cystéine (composition chimique)</term><term>Cystéine (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Methionine Sulfoxide Reductases (composition chimique)</term><term>Methionine Sulfoxide Reductases (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Cysteine</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Cystéine</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Clostridium</term><term>Cysteine</term><term>Glutaredoxins</term><term>Methionine Sulfoxide Reductases</term><term>Sulfenic Acids</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acides sulféniques</term><term>Clostridium</term><term>Cystéine</term><term>Glutarédoxines</term><term>Methionine Sulfoxide Reductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Clostridium</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Clostridium</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Clostridium</term><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione</term><term>Methionine Sulfoxide Reductases</term><term>Sulfenic Acids</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sulféniques</term><term>Clostridium</term><term>Cystéine</term><term>Glutarédoxines</term><term>Glutathion</term><term>Methionine Sulfoxide Reductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Kinetics</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (Grx), a major redox regulator, can act as a reductant of methionine sulfoxide reductase A (MsrA). However, the biochemical mechanisms involved in MsrA activity regeneration by Grx remain largely unknown. In this study, we investigated the regeneration mechanism of 1-Cys type Clostridium oremlandii MsrA (cMsrA) lacking a resolving Cys residue in a Grx-dependent assay. Kinetic analysis showed that cMsrA could be reduced by both monothiol and dithiol Grxs as efficiently as by in vitro reductant dithiothreitol. Our data revealed that the catalytic Cys sulfenic acid intermediate is not glutathionylated in the presence of the substrate, and that Grx instead directly formed a complex with cMsrA. Mass spectrometry analysis identified a disulfide bond between the N-terminal catalytic Cys of the active site of Grx and the catalytic Cys of cMsrA. This mixed disulfide bond could be resolved by glutathione. Based on these findings, we propose a model for regeneration of 1-Cys type cMsrA by Grx that involves no glutathionylation on the catalytic Cys of cMsrA. This mechanism contrasts with that of the previously known 1-Cys type MsrB.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25600814</PMID><DateCompleted><Year>2015</Year><Month>04</Month><Day>17</Day></DateCompleted><DateRevised><Year>2015</Year><Month>02</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>457</Volume><Issue>4</Issue><PubDate><Year>2015</Year><Month>Feb</Month><Day>20</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>567-71</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2015.01.025</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(15)00047-9</ELocationID><Abstract><AbstractText>Glutaredoxin (Grx), a major redox regulator, can act as a reductant of methionine sulfoxide reductase A (MsrA). However, the biochemical mechanisms involved in MsrA activity regeneration by Grx remain largely unknown. In this study, we investigated the regeneration mechanism of 1-Cys type Clostridium oremlandii MsrA (cMsrA) lacking a resolving Cys residue in a Grx-dependent assay. Kinetic analysis showed that cMsrA could be reduced by both monothiol and dithiol Grxs as efficiently as by in vitro reductant dithiothreitol. Our data revealed that the catalytic Cys sulfenic acid intermediate is not glutathionylated in the presence of the substrate, and that Grx instead directly formed a complex with cMsrA. Mass spectrometry analysis identified a disulfide bond between the N-terminal catalytic Cys of the active site of Grx and the catalytic Cys of cMsrA. This mixed disulfide bond could be resolved by glutathione. Based on these findings, we propose a model for regeneration of 1-Cys type cMsrA by Grx that involves no glutathionylation on the catalytic Cys of cMsrA. This mechanism contrasts with that of the previously known 1-Cys type MsrB.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Moon-Jung</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jeong</LastName><ForeName>Jaeho</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jeong</LastName><ForeName>Jihye</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Kwang Yeon</ForeName><Initials>KY</Initials><AffiliationInfo><Affiliation>Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University, Seoul 136-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Kong-Joo</ForeName><Initials>KJ</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 120-750, Republic of Korea. Electronic address: kjl@ewha.ac.kr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Hwa-Young</ForeName><Initials>HY</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Republic of Korea. Electronic address: hykim@ynu.ac.kr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>01</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013434">Sulfenic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="D051150">Methionine Sulfoxide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>FB8KIA847T</RegistryNumber><NameOfSubstance UI="C100870">cysteinesulfenic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003013" MajorTopicYN="N">Clostridium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051150" MajorTopicYN="N">Methionine Sulfoxide Reductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013434" MajorTopicYN="N">Sulfenic Acids</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">1-Cys MsrA</Keyword><Keyword MajorTopicYN="N">Disulfide bond</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Glutathionylation</Keyword><Keyword MajorTopicYN="N">Regeneration</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>12</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>01</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>1</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>1</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>4</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25600814</ArticleId><ArticleId IdType="pii">S0006-291X(15)00047-9</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2015.01.025</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><country name="Corée du Sud"><noRegion><name sortKey="Kim, Moon Jung" sort="Kim, Moon Jung" uniqKey="Kim M" first="Moon-Jung" last="Kim">Moon-Jung Kim</name></noRegion><name sortKey="Hwang, Kwang Yeon" sort="Hwang, Kwang Yeon" uniqKey="Hwang K" first="Kwang Yeon" last="Hwang">Kwang Yeon Hwang</name><name sortKey="Jeong, Jaeho" sort="Jeong, Jaeho" uniqKey="Jeong J" first="Jaeho" last="Jeong">Jaeho Jeong</name><name sortKey="Jeong, Jihye" sort="Jeong, Jihye" uniqKey="Jeong J" first="Jihye" last="Jeong">Jihye Jeong</name><name sortKey="Kim, Hwa Young" sort="Kim, Hwa Young" uniqKey="Kim H" first="Hwa-Young" last="Kim">Hwa-Young Kim</name><name sortKey="Lee, Kong Joo" sort="Lee, Kong Joo" uniqKey="Lee K" first="Kong-Joo" last="Lee">Kong-Joo Lee</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:25600814" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |