Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P1B-type ATPase, ATP7B.
Identifieur interne : 000060 ( Main/Exploration ); précédent : 000059; suivant : 000061Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P1B-type ATPase, ATP7B.
Auteurs : Shadi Maghool [Australie] ; Sharon La Fontaine [Australie] ; Blaine R. Roberts [Australie, États-Unis] ; Ann H. Kwan [Australie] ; Megan J. Maher [Australie]Source :
- Scientific reports [ 2045-2322 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- Copper (metabolism), Copper Transport Proteins (genetics), Copper Transport Proteins (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Humans (MeSH), Magnetic Resonance Spectroscopy (MeSH), Molecular Chaperones (genetics), Molecular Chaperones (metabolism), Protein Binding (MeSH), Protein Structure, Quaternary (MeSH).
- MESH :
- chemical , genetics : Copper Transport Proteins, Glutaredoxins, Molecular Chaperones.
- chemical , metabolism : Copper, Copper Transport Proteins, Glutaredoxins, Molecular Chaperones.
- Humans, Magnetic Resonance Spectroscopy, Protein Binding, Protein Structure, Quaternary.
Abstract
Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P1B-type ATPase ATP7B and to determine the thermodynamic factors that underpin this activity. hGrx1 can transfer Cu to the metallochaperone Atox1 and to the MBDs 5-6 of ATP7B (WLN5-6). This exchange is irreversible. In a mixture of the three proteins, Cu is delivered to the WLN5-6 preferentially, despite the presence of Atox1. This preferential Cu exchange appears to be driven by both the thermodynamics of the interactions between the proteins pairs and of the proteins with Cu(I). Crucially, protein-protein interactions between hGrx1, Atox1 and WLN5-6 were detected by NMR spectroscopy both in the presence and absence of Cu at a common interface. This study augments the possible activities of hGrx1 in intracellular Cu homeostasis and suggests a potential redundancy in this system, where hGrx1 has the potential to act under cellular conditions where the activity of Atox1 in Cu regulation is attenuated.
DOI: 10.1038/s41598-020-60953-z
PubMed: 32139726
PubMed Central: PMC7057996
Affiliations:
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Kwan</name><affiliation wicri:level="1"><nlm:affiliation>School of Life and Environmental Sciences and University of Sydney Nano Institute, Sydney, NSW, Australia. ann.kwan@sydney.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Life and Environmental Sciences and University of Sydney Nano Institute, Sydney, NSW</wicri:regionArea><wicri:noRegion>NSW</wicri:noRegion></affiliation></author><author><name sortKey="Maher, Megan J" sort="Maher, Megan J" uniqKey="Maher M" first="Megan J" last="Maher">Megan J. Maher</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia. megan.maher@unimelb.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC</wicri:regionArea><wicri:noRegion>VIC</wicri:noRegion></affiliation><affiliation wicri:level="4"><nlm:affiliation>School of Chemistry and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Australia. megan.maher@unimelb.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Copper (metabolism)</term><term>Copper Transport Proteins (genetics)</term><term>Copper Transport Proteins (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Humans (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Molecular Chaperones (genetics)</term><term>Molecular Chaperones (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Structure, Quaternary (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chaperons moléculaires (génétique)</term><term>Chaperons moléculaires (métabolisme)</term><term>Cuivre (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Structure quaternaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Copper Transport Proteins</term><term>Glutaredoxins</term><term>Molecular Chaperones</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Copper Transport Proteins</term><term>Glutaredoxins</term><term>Molecular Chaperones</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Chaperons moléculaires</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chaperons moléculaires</term><term>Cuivre</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Magnetic Resonance Spectroscopy</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison aux protéines</term><term>Spectroscopie par résonance magnétique</term><term>Structure quaternaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P<sub>1B</sub>-type ATPase ATP7B and to determine the thermodynamic factors that underpin this activity. hGrx1 can transfer Cu to the metallochaperone Atox1 and to the MBDs 5-6 of ATP7B (WLN5-6). This exchange is irreversible. In a mixture of the three proteins, Cu is delivered to the WLN5-6 preferentially, despite the presence of Atox1. This preferential Cu exchange appears to be driven by both the thermodynamics of the interactions between the proteins pairs and of the proteins with Cu(I). Crucially, protein-protein interactions between hGrx1, Atox1 and WLN5-6 were detected by NMR spectroscopy both in the presence and absence of Cu at a common interface. This study augments the possible activities of hGrx1 in intracellular Cu homeostasis and suggests a potential redundancy in this system, where hGrx1 has the potential to act under cellular conditions where the activity of Atox1 in Cu regulation is attenuated.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32139726</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>03</Month><Day>05</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P<sub>1B</sub>-type ATPase, ATP7B.</ArticleTitle><Pagination><MedlinePgn>4157</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-020-60953-z</ELocationID><Abstract><AbstractText>Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P<sub>1B</sub>-type ATPase ATP7B and to determine the thermodynamic factors that underpin this activity. hGrx1 can transfer Cu to the metallochaperone Atox1 and to the MBDs 5-6 of ATP7B (WLN5-6). This exchange is irreversible. In a mixture of the three proteins, Cu is delivered to the WLN5-6 preferentially, despite the presence of Atox1. This preferential Cu exchange appears to be driven by both the thermodynamics of the interactions between the proteins pairs and of the proteins with Cu(I). Crucially, protein-protein interactions between hGrx1, Atox1 and WLN5-6 were detected by NMR spectroscopy both in the presence and absence of Cu at a common interface. This study augments the possible activities of hGrx1 in intracellular Cu homeostasis and suggests a potential redundancy in this system, where hGrx1 has the potential to act under cellular conditions where the activity of Atox1 in Cu regulation is attenuated.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Maghool</LastName><ForeName>Shadi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fontaine</LastName><ForeName>Sharon La</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Life and Environmental Sciences, Deakin University, Geelong, VIC, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>The Florey Institute of Neuroscience, The University of Melbourne, Parkville, VIC, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roberts</LastName><ForeName>Blaine R</ForeName><Initials>BR</Initials><AffiliationInfo><Affiliation>The Florey Institute of Neuroscience, The University of Melbourne, Parkville, VIC, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, 30322, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kwan</LastName><ForeName>Ann H</ForeName><Initials>AH</Initials><AffiliationInfo><Affiliation>School of Life and Environmental Sciences and University of Sydney Nano Institute, Sydney, NSW, Australia. ann.kwan@sydney.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maher</LastName><ForeName>Megan J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC, Australia. megan.maher@unimelb.edu.au.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Chemistry and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Australia. megan.maher@unimelb.edu.au.</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>2020</Year><Month>03</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C474500">ATOX1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000079922">Copper Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018832">Molecular Chaperones</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000079922" MajorTopicYN="N">Copper Transport Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018832" MajorTopicYN="N">Molecular Chaperones</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020836" 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IdType="pubmed">11823463</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>États-Unis</li></country><region><li>Victoria (État)</li></region><settlement><li>Melbourne</li></settlement><orgName><li>Université de Melbourne</li></orgName></list><tree><country name="Australie"><noRegion><name sortKey="Maghool, Shadi" sort="Maghool, Shadi" uniqKey="Maghool S" first="Shadi" last="Maghool">Shadi Maghool</name></noRegion><name sortKey="Fontaine, Sharon La" sort="Fontaine, Sharon La" uniqKey="Fontaine S" first="Sharon La" last="Fontaine">Sharon La Fontaine</name><name sortKey="Fontaine, Sharon La" sort="Fontaine, Sharon La" uniqKey="Fontaine S" first="Sharon La" last="Fontaine">Sharon La Fontaine</name><name sortKey="Kwan, Ann H" sort="Kwan, Ann H" uniqKey="Kwan A" first="Ann H" last="Kwan">Ann H. Kwan</name><name sortKey="Maher, Megan J" sort="Maher, Megan J" uniqKey="Maher M" first="Megan J" last="Maher">Megan J. Maher</name><name sortKey="Maher, Megan J" sort="Maher, Megan J" uniqKey="Maher M" first="Megan J" last="Maher">Megan J. Maher</name><name sortKey="Roberts, Blaine R" sort="Roberts, Blaine R" uniqKey="Roberts B" first="Blaine R" last="Roberts">Blaine R. Roberts</name></country><country name="États-Unis"><noRegion><name sortKey="Roberts, Blaine R" sort="Roberts, Blaine R" uniqKey="Roberts B" first="Blaine R" last="Roberts">Blaine R. Roberts</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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