Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein.
Identifieur interne : 000460 ( Main/Exploration ); précédent : 000459; suivant : 000461Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein.
Auteurs : Gang Liu [République populaire de Chine] ; Yongwei Wang [République populaire de Chine] ; Gregory J. Anderson [Australie] ; Clara Camaschella [Italie] ; Yanzhong Chang [République populaire de Chine] ; Guangjun Nie [République populaire de Chine]Source :
- Journal of cellular biochemistry [ 1097-4644 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Ferrosulfoprotéines, Glutarédoxines, Mutation.
- métabolisme : Ferrosulfoprotéines, Glutarédoxines.
- Humains, Liaison aux protéines, Lignée cellulaire.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Glutaredoxins, Iron-Sulfur Proteins.
- chemical , metabolism : Glutaredoxins, Iron-Sulfur Proteins.
- genetics : Mutation.
- Cell Line, Humans, Protein Binding.
Abstract
Glutaredoxin 5 (GLRX5) is a 156 amino acid mitochondrial protein that plays an essential role in mitochondrial iron-sulfur cluster transfer. Mutations in this protein were reported to result in sideroblastic anemia and variant nonketotic hyperglycinemia in human. Recently, we have characterized a Chinese congenital sideroblastic anemia patient who has two compound heterozygous missense mutations (c. 301 A>C and c. 443 T>C) in his GLRX5 gene. Herein, we developed a GLRX5 knockout K562 cell line and studied the biochemical functions of the identified pathogenic mutations and other conserved amino acids with predicted essential functions. We observed that the K101Q mutation (due to c. 301 A>C mutation) may prevent the binding of [Fe-S] to GLRX5 protein, while L148S (due to c. 443 T>C mutation) may interfere with [Fe-S] transfer from GLRX5 to iron regulatory protein 1 (IRP1), mitochondrial aconitase (m-aconitase) and ferrochelatase. We also demonstrated that L148S is functionally complementary to the K51del mutant with respect to Fe/S-ferrochelatase, Fe/S-IRP1, Fe/S-succinate dehydrogenase, and Fe/S-m-aconitase biosynthesis and lipoylation of pyruvate dehydrogenase complex and α-ketoglutarate dehydrogenase complex. Furthermore, we demonstrated that the mutations of highly conserved amino acid residues in GLRX5 protein can have different effects on downstream Fe/S proteins. Collectively, our current work demonstrates that GLRX5 protein is multifunctional in [Fe-S] protein synthesis and maturation and defects of the different amino acids of the protein will lead to distinct effects on downstream Fe/S biosynthesis.
DOI: 10.1002/jcb.25267
PubMed: 26100117
Affiliations:
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sortKey="Chang, Yanzhong" sort="Chang, Yanzhong" uniqKey="Chang Y" first="Yanzhong" last="Chang">Yanzhong Chang</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province</wicri:regionArea><wicri:noRegion>Hebei Province</wicri:noRegion></affiliation></author><author><name sortKey="Nie, Guangjun" sort="Nie, Guangjun" uniqKey="Nie G" first="Guangjun" last="Nie">Guangjun Nie</name><affiliation wicri:level="1"><nlm:affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190</wicri:regionArea><wicri:noRegion>100190</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26100117</idno><idno type="pmid">26100117</idno><idno type="doi">10.1002/jcb.25267</idno><idno type="wicri:Area/Main/Corpus">000520</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000520</idno><idno type="wicri:Area/Main/Curation">000520</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000520</idno><idno type="wicri:Area/Main/Exploration">000520</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein.</title><author><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name><affiliation wicri:level="1"><nlm:affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190</wicri:regionArea><wicri:noRegion>100190</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Yongwei" sort="Wang, Yongwei" uniqKey="Wang Y" first="Yongwei" last="Wang">Yongwei Wang</name><affiliation wicri:level="1"><nlm:affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190</wicri:regionArea><wicri:noRegion>100190</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province</wicri:regionArea><wicri:noRegion>Hebei Province</wicri:noRegion></affiliation></author><author><name sortKey="Anderson, Gregory J" sort="Anderson, Gregory J" uniqKey="Anderson G" first="Gregory J" last="Anderson">Gregory J. Anderson</name><affiliation wicri:level="1"><nlm:affiliation>Iron Metabolism Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Iron Metabolism Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland</wicri:regionArea><wicri:noRegion>Queensland</wicri:noRegion></affiliation></author><author><name sortKey="Camaschella, Clara" sort="Camaschella, Clara" uniqKey="Camaschella C" first="Clara" last="Camaschella">Clara Camaschella</name><affiliation wicri:level="3"><nlm:affiliation>Vita-Salute University, and IRCCS San Raffaele Scientific Institute, Milan, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Vita-Salute University, and IRCCS San Raffaele Scientific Institute, Milan</wicri:regionArea><placeName><settlement type="city">Milan</settlement><region nuts="2">Lombardie</region></placeName></affiliation></author><author><name sortKey="Chang, Yanzhong" sort="Chang, Yanzhong" uniqKey="Chang Y" first="Yanzhong" last="Chang">Yanzhong Chang</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province</wicri:regionArea><wicri:noRegion>Hebei Province</wicri:noRegion></affiliation></author><author><name sortKey="Nie, Guangjun" sort="Nie, Guangjun" uniqKey="Nie G" first="Guangjun" last="Nie">Guangjun Nie</name><affiliation wicri:level="1"><nlm:affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190</wicri:regionArea><wicri:noRegion>100190</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of cellular biochemistry</title><idno type="eISSN">1097-4644</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line (MeSH)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (genetics)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Mutation (genetics)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Ferrosulfoprotéines (génétique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Mutation (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin 5 (GLRX5) is a 156 amino acid mitochondrial protein that plays an essential role in mitochondrial iron-sulfur cluster transfer. Mutations in this protein were reported to result in sideroblastic anemia and variant nonketotic hyperglycinemia in human. Recently, we have characterized a Chinese congenital sideroblastic anemia patient who has two compound heterozygous missense mutations (c. 301 A>C and c. 443 T>C) in his GLRX5 gene. Herein, we developed a GLRX5 knockout K562 cell line and studied the biochemical functions of the identified pathogenic mutations and other conserved amino acids with predicted essential functions. We observed that the K101Q mutation (due to c. 301 A>C mutation) may prevent the binding of [Fe-S] to GLRX5 protein, while L148S (due to c. 443 T>C mutation) may interfere with [Fe-S] transfer from GLRX5 to iron regulatory protein 1 (IRP1), mitochondrial aconitase (m-aconitase) and ferrochelatase. We also demonstrated that L148S is functionally complementary to the K51del mutant with respect to Fe/S-ferrochelatase, Fe/S-IRP1, Fe/S-succinate dehydrogenase, and Fe/S-m-aconitase biosynthesis and lipoylation of pyruvate dehydrogenase complex and α-ketoglutarate dehydrogenase complex. Furthermore, we demonstrated that the mutations of highly conserved amino acid residues in GLRX5 protein can have different effects on downstream Fe/S proteins. Collectively, our current work demonstrates that GLRX5 protein is multifunctional in [Fe-S] protein synthesis and maturation and defects of the different amino acids of the protein will lead to distinct effects on downstream Fe/S biosynthesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26100117</PMID><DateCompleted><Year>2016</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-4644</ISSN><JournalIssue CitedMedium="Internet"><Volume>117</Volume><Issue>1</Issue><PubDate><Year>2016</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Journal of cellular biochemistry</Title><ISOAbbreviation>J Cell Biochem</ISOAbbreviation></Journal><ArticleTitle>Functional Analysis of GLRX5 Mutants Reveals Distinct Functionalities of GLRX5 Protein.</ArticleTitle><Pagination><MedlinePgn>207-17</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/jcb.25267</ELocationID><Abstract><AbstractText>Glutaredoxin 5 (GLRX5) is a 156 amino acid mitochondrial protein that plays an essential role in mitochondrial iron-sulfur cluster transfer. Mutations in this protein were reported to result in sideroblastic anemia and variant nonketotic hyperglycinemia in human. Recently, we have characterized a Chinese congenital sideroblastic anemia patient who has two compound heterozygous missense mutations (c. 301 A>C and c. 443 T>C) in his GLRX5 gene. Herein, we developed a GLRX5 knockout K562 cell line and studied the biochemical functions of the identified pathogenic mutations and other conserved amino acids with predicted essential functions. We observed that the K101Q mutation (due to c. 301 A>C mutation) may prevent the binding of [Fe-S] to GLRX5 protein, while L148S (due to c. 443 T>C mutation) may interfere with [Fe-S] transfer from GLRX5 to iron regulatory protein 1 (IRP1), mitochondrial aconitase (m-aconitase) and ferrochelatase. We also demonstrated that L148S is functionally complementary to the K51del mutant with respect to Fe/S-ferrochelatase, Fe/S-IRP1, Fe/S-succinate dehydrogenase, and Fe/S-m-aconitase biosynthesis and lipoylation of pyruvate dehydrogenase complex and α-ketoglutarate dehydrogenase complex. Furthermore, we demonstrated that the mutations of highly conserved amino acid residues in GLRX5 protein can have different effects on downstream Fe/S proteins. Collectively, our current work demonstrates that GLRX5 protein is multifunctional in [Fe-S] protein synthesis and maturation and defects of the different amino acids of the protein will lead to distinct effects on downstream Fe/S biosynthesis.</AbstractText><CopyrightInformation>© 2015 Wiley Periodicals, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Gang</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yongwei</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Gregory J</ForeName><Initials>GJ</Initials><AffiliationInfo><Affiliation>Iron Metabolism Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camaschella</LastName><ForeName>Clara</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Vita-Salute University, and IRCCS San Raffaele Scientific Institute, Milan, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Yanzhong</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang, 050024, Hebei Province, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nie</LastName><ForeName>Guangjun</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology, No.11 Zhongguancun Beiyitiao, Beijing, 100190, China.</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Cell Biochem</MedlineTA><NlmUniqueID>8205768</NlmUniqueID><ISSNLinking>0730-2312</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></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="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">GLRX5</Keyword><Keyword MajorTopicYN="N">IRON-SULFUR CLUSTER BIOSYNTHESIS</Keyword><Keyword MajorTopicYN="N">MUTATIONS</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>05</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>06</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>6</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>6</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26100117</ArticleId><ArticleId IdType="doi">10.1002/jcb.25267</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Italie</li><li>République populaire de Chine</li></country><region><li>Lombardie</li></region><settlement><li>Milan</li></settlement></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Liu, Gang" sort="Liu, Gang" uniqKey="Liu G" first="Gang" last="Liu">Gang Liu</name></noRegion><name sortKey="Chang, Yanzhong" sort="Chang, Yanzhong" uniqKey="Chang Y" first="Yanzhong" last="Chang">Yanzhong Chang</name><name sortKey="Nie, Guangjun" sort="Nie, Guangjun" uniqKey="Nie G" first="Guangjun" last="Nie">Guangjun Nie</name><name sortKey="Wang, Yongwei" sort="Wang, Yongwei" uniqKey="Wang Y" first="Yongwei" last="Wang">Yongwei Wang</name><name sortKey="Wang, Yongwei" sort="Wang, Yongwei" uniqKey="Wang Y" first="Yongwei" last="Wang">Yongwei Wang</name></country><country name="Australie"><noRegion><name sortKey="Anderson, Gregory J" sort="Anderson, Gregory J" uniqKey="Anderson G" first="Gregory J" last="Anderson">Gregory J. Anderson</name></noRegion></country><country name="Italie"><region name="Lombardie"><name sortKey="Camaschella, Clara" sort="Camaschella, Clara" uniqKey="Camaschella C" first="Clara" last="Camaschella">Clara Camaschella</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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