Identification of IscU residues critical for de novo iron-sulfur cluster assembly.
Identifieur interne : 000235 ( Main/Exploration ); précédent : 000234; suivant : 000236Identification of IscU residues critical for de novo iron-sulfur cluster assembly.
Auteurs : Naoyuki Tanaka [Japon] ; Eiki Yuda [Japon] ; Takashi Fujishiro [Japon] ; Kei Hirabayashi [Japon] ; Kei Wada [Japon] ; Yasuhiro Takahashi [Japon]Source :
- Molecular microbiology [ 1365-2958 ] ; 2019.
Descripteurs français
- KwdFr :
- Acides aminés (génétique), Conformation des protéines (MeSH), Escherichia coli (métabolisme), Fer (métabolisme), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Ferrosulfoprotéines (ultrastructure), Liaison aux protéines (MeSH), Ligands (MeSH), Mutation (génétique), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Protéines Escherichia coli (ultrastructure), Protéines bactériennes (métabolisme), Relation structure-activité (MeSH), Soufre (métabolisme).
- MESH :
- génétique : Acides aminés, Ferrosulfoprotéines, Mutation, Protéines Escherichia coli.
- métabolisme : Escherichia coli, Fer, Ferrosulfoprotéines, Protéines Escherichia coli, Protéines bactériennes, Soufre.
- ultrastructure : Conformation des protéines, Ferrosulfoprotéines, Liaison aux protéines, Ligands, Protéines Escherichia coli, Relation structure-activité.
English descriptors
- KwdEn :
- Amino Acids (genetics), Bacterial Proteins (metabolism), Escherichia coli (metabolism), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Escherichia coli Proteins (ultrastructure), Iron (metabolism), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Iron-Sulfur Proteins (ultrastructure), Ligands (MeSH), Mutation (genetics), Protein Binding (MeSH), Protein Conformation (MeSH), Structure-Activity Relationship (MeSH), Sulfur (metabolism).
- MESH :
- chemical , genetics : Amino Acids, Escherichia coli Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Bacterial Proteins, Escherichia coli Proteins, Iron, Iron-Sulfur Proteins, Sulfur.
- genetics : Mutation.
- metabolism : Escherichia coli.
- chemical , ultrastructure : Escherichia coli Proteins, Iron-Sulfur Proteins.
- chemical : Ligands, Protein Binding, Protein Conformation, Structure-Activity Relationship.
Abstract
IscU is a central component of the ISC machinery and serves as a scaffold for the de novo assembly of iron-sulfur (Fe-S) clusters prior to their delivery to target apo-Fe-S proteins. However, the molecular mechanism is not yet fully understood. In this study, we have conducted mutational analysis of E. coli IscU using the recently developed genetic complementation system of a mutant that can survive without Fe-S clusters. The Fe-S cluster ligands (C37, C63, H105, C106) and the proximal D39 and K103 residues are essential for in vivo function of IscU and could not be substituted with any other amino acids. Furthermore, we found that substitution of Y3, a strictly conserved residue among IscU homologs, abolished in vivo functions. Surprisingly, a second-site suppressor mutation in IscS (A349V) reverted the defect caused by IscU Y3 substitutions. Biochemical analysis revealed that IscU Y3 was crucial for functional interaction with IscS and sulfur transfer between the two proteins. Our findings suggest that the critical role of IscU Y3 is linked to the conformational dynamics of the flexible loop of IscS, which is required for the ingenious sulfur transfer to IscU.
DOI: 10.1111/mmi.14392
PubMed: 31532036
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570</wicri:regionArea><wicri:noRegion>338-8570</wicri:noRegion></affiliation></author><author><name sortKey="Yuda, Eiki" sort="Yuda, Eiki" uniqKey="Yuda E" first="Eiki" last="Yuda">Eiki Yuda</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570</wicri:regionArea><wicri:noRegion>338-8570</wicri:noRegion></affiliation></author><author><name sortKey="Fujishiro, Takashi" sort="Fujishiro, Takashi" uniqKey="Fujishiro T" first="Takashi" last="Fujishiro">Takashi 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889-1692</wicri:regionArea><wicri:noRegion>889-1692</wicri:noRegion></affiliation></author><author><name sortKey="Wada, Kei" sort="Wada, Kei" uniqKey="Wada K" first="Kei" last="Wada">Kei Wada</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Sciences, University of Miyazaki, Miyazaki, 889-1692, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Medical Sciences, University of Miyazaki, Miyazaki, 889-1692</wicri:regionArea><wicri:noRegion>889-1692</wicri:noRegion></affiliation></author><author><name sortKey="Takahashi, Yasuhiro" sort="Takahashi, Yasuhiro" uniqKey="Takahashi Y" first="Yasuhiro" last="Takahashi">Yasuhiro Takahashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570</wicri:regionArea><wicri:noRegion>338-8570</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecular microbiology</title><idno type="eISSN">1365-2958</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acids (genetics)</term><term>Bacterial Proteins (metabolism)</term><term>Escherichia coli (metabolism)</term><term>Escherichia coli Proteins (genetics)</term><term>Escherichia coli Proteins (metabolism)</term><term>Escherichia coli Proteins (ultrastructure)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (genetics)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Iron-Sulfur Proteins (ultrastructure)</term><term>Ligands (MeSH)</term><term>Mutation (genetics)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term><term>Sulfur (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (génétique)</term><term>Conformation des protéines (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (génétique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Ferrosulfoprotéines (ultrastructure)</term><term>Liaison aux protéines (MeSH)</term><term>Ligands (MeSH)</term><term>Mutation (génétique)</term><term>Protéines Escherichia coli (génétique)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Protéines Escherichia coli (ultrastructure)</term><term>Protéines bactériennes (métabolisme)</term><term>Relation structure-activité (MeSH)</term><term>Soufre (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acids</term><term>Escherichia coli Proteins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Escherichia coli Proteins</term><term>Iron</term><term>Iron-Sulfur Proteins</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acides aminés</term><term>Ferrosulfoprotéines</term><term>Mutation</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Fer</term><term>Ferrosulfoprotéines</term><term>Protéines Escherichia coli</term><term>Protéines bactériennes</term><term>Soufre</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Escherichia coli Proteins</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Ligands</term><term>Protein Binding</term><term>Protein Conformation</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Conformation des protéines</term><term>Ferrosulfoprotéines</term><term>Liaison aux protéines</term><term>Ligands</term><term>Protéines Escherichia coli</term><term>Relation structure-activité</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">IscU is a central component of the ISC machinery and serves as a scaffold for the de novo assembly of iron-sulfur (Fe-S) clusters prior to their delivery to target apo-Fe-S proteins. However, the molecular mechanism is not yet fully understood. In this study, we have conducted mutational analysis of E. coli IscU using the recently developed genetic complementation system of a mutant that can survive without Fe-S clusters. The Fe-S cluster ligands (C37, C63, H105, C106) and the proximal D39 and K103 residues are essential for in vivo function of IscU and could not be substituted with any other amino acids. Furthermore, we found that substitution of Y3, a strictly conserved residue among IscU homologs, abolished in vivo functions. Surprisingly, a second-site suppressor mutation in IscS (A349V) reverted the defect caused by IscU Y3 substitutions. Biochemical analysis revealed that IscU Y3 was crucial for functional interaction with IscS and sulfur transfer between the two proteins. Our findings suggest that the critical role of IscU Y3 is linked to the conformational dynamics of the flexible loop of IscS, which is required for the ingenious sulfur transfer to IscU.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31532036</PMID><DateCompleted><Year>2020</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>06</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-2958</ISSN><JournalIssue CitedMedium="Internet"><Volume>112</Volume><Issue>6</Issue><PubDate><Year>2019</Year><Month>12</Month></PubDate></JournalIssue><Title>Molecular microbiology</Title><ISOAbbreviation>Mol Microbiol</ISOAbbreviation></Journal><ArticleTitle>Identification of IscU residues critical for de novo iron-sulfur cluster assembly.</ArticleTitle><Pagination><MedlinePgn>1769-1783</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/mmi.14392</ELocationID><Abstract><AbstractText>IscU is a central component of the ISC machinery and serves as a scaffold for the de novo assembly of iron-sulfur (Fe-S) clusters prior to their delivery to target apo-Fe-S proteins. However, the molecular mechanism is not yet fully understood. In this study, we have conducted mutational analysis of E. coli IscU using the recently developed genetic complementation system of a mutant that can survive without Fe-S clusters. The Fe-S cluster ligands (C37, C63, H105, C106) and the proximal D39 and K103 residues are essential for in vivo function of IscU and could not be substituted with any other amino acids. Furthermore, we found that substitution of Y3, a strictly conserved residue among IscU homologs, abolished in vivo functions. Surprisingly, a second-site suppressor mutation in IscS (A349V) reverted the defect caused by IscU Y3 substitutions. Biochemical analysis revealed that IscU Y3 was crucial for functional interaction with IscS and sulfur transfer between the two proteins. Our findings suggest that the critical role of IscU Y3 is linked to the conformational dynamics of the flexible loop of IscS, which is required for the ingenious sulfur transfer to IscU.</AbstractText><CopyrightInformation>© 2019 John Wiley & Sons Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tanaka</LastName><ForeName>Naoyuki</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yuda</LastName><ForeName>Eiki</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fujishiro</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0001-7967-8380</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hirabayashi</LastName><ForeName>Kei</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Medical Sciences, University of Miyazaki, Miyazaki, 889-1692, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wada</LastName><ForeName>Kei</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Medical Sciences, University of Miyazaki, Miyazaki, 889-1692, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takahashi</LastName><ForeName>Yasuhiro</ForeName><Initials>Y</Initials><Identifier Source="ORCID">0000-0002-0588-6045</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</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>2019</Year><Month>10</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Microbiol</MedlineTA><NlmUniqueID>8712028</NlmUniqueID><ISSNLinking>0950-382X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>9</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31532036</ArticleId><ArticleId IdType="doi">10.1111/mmi.14392</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Adrover, M., Howes, B.D., Iannuzzi, C., Smulevich, G. and Pastore, A. 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