Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.
Identifieur interne : 000137 ( Main/Exploration ); précédent : 000136; suivant : 000138Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.
Auteurs : Sakiko Sato [Japon] ; Yumeka Matsushima [Japon] ; Miaki Kanazawa [Japon] ; Naoyuki Tanaka [Japon] ; Takashi Fujishiro [Japon] ; Kouhei Kunichika [Japon] ; Ryosuke Nakamura [Japon] ; Hiroaki Tomioka [Japon] ; Kei Wada [Japon] ; Yasuhiro Takahashi [Japon]Source :
- Molecular microbiology [ 1365-2958 ] ; 2020.
Abstract
IscU is a central component of the ISC machinery and serves as a scaffold for de novo assembly of Fe-S clusters. The dedicated chaperone system composed of the Hsp70-chaperone HscA and the J-protein cochaperone HscB synergistically interacts with IscU and facilitates cluster transfer from IscU to recipient apo-proteins. Here we report that the otherwise essential roles of HscA and HscB can be bypassed in vivo by a number of single amino acid substitutions in IscU. CD spectroscopic studies of the variant IscU proteins capable of this bypass activity revealed dynamic interconversion between two conformations: the denatured (D) and the structured (S) state in the absence and presence of Zn2+ , respectively, which was far more prominent than interconversion observed in wild-type IscU. Furthermore, we found that neither the S-shifted (more structured) variants of IscU nor the perpetually denatured variants could perform their in vivo role regardless of whether the chaperone system was present or not. The present study thus provides for the first time evidence that an in vivo D-state of IscU exists and implies that conformational interconversion between the S- and D-states of the scaffolding protein is a fundamental requirement for the assembly and transfer of the Fe-S cluster.
DOI: 10.1111/mmi.14646
PubMed: 33202070
Affiliations:
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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="Matsushima, Yumeka" sort="Matsushima, Yumeka" uniqKey="Matsushima Y" first="Yumeka" last="Matsushima">Yumeka Matsushima</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="Kanazawa, Miaki" sort="Kanazawa, Miaki" uniqKey="Kanazawa M" first="Miaki" last="Kanazawa">Miaki Kanazawa</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="Tanaka, Naoyuki" sort="Tanaka, Naoyuki" uniqKey="Tanaka N" first="Naoyuki" last="Tanaka">Naoyuki Tanaka</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 Fujishiro</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="Kunichika, Kouhei" sort="Kunichika, Kouhei" uniqKey="Kunichika K" first="Kouhei" last="Kunichika">Kouhei Kunichika</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="Nakamura, Ryosuke" sort="Nakamura, Ryosuke" uniqKey="Nakamura R" first="Ryosuke" last="Nakamura">Ryosuke Nakamura</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="Tomioka, Hiroaki" sort="Tomioka, Hiroaki" uniqKey="Tomioka H" first="Hiroaki" last="Tomioka">Hiroaki Tomioka</name><affiliation wicri:level="1"><nlm:affiliation>Department of Science Education, Graduate School of Education, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Science Education, Graduate School of Education, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570</wicri:regionArea><wicri:noRegion>338-8570</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="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></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 de novo assembly of Fe-S clusters. The dedicated chaperone system composed of the Hsp70-chaperone HscA and the J-protein cochaperone HscB synergistically interacts with IscU and facilitates cluster transfer from IscU to recipient apo-proteins. Here we report that the otherwise essential roles of HscA and HscB can be bypassed in vivo by a number of single amino acid substitutions in IscU. CD spectroscopic studies of the variant IscU proteins capable of this bypass activity revealed dynamic interconversion between two conformations: the denatured (D) and the structured (S) state in the absence and presence of Zn<sup>2+</sup> , respectively, which was far more prominent than interconversion observed in wild-type IscU. Furthermore, we found that neither the S-shifted (more structured) variants of IscU nor the perpetually denatured variants could perform their in vivo role regardless of whether the chaperone system was present or not. The present study thus provides for the first time evidence that an in vivo D-state of IscU exists and implies that conformational interconversion between the S- and D-states of the scaffolding protein is a fundamental requirement for the assembly and transfer of the Fe-S cluster.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33202070</PMID><DateRevised><Year>2020</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-2958</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Nov</Month><Day>17</Day></PubDate></JournalIssue><Title>Molecular microbiology</Title><ISOAbbreviation>Mol Microbiol</ISOAbbreviation></Journal><ArticleTitle>Evidence for dynamic in vivo interconversion of the conformational states of IscU during iron-sulfur cluster biosynthesis.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/mmi.14646</ELocationID><Abstract><AbstractText>IscU is a central component of the ISC machinery and serves as a scaffold for de novo assembly of Fe-S clusters. The dedicated chaperone system composed of the Hsp70-chaperone HscA and the J-protein cochaperone HscB synergistically interacts with IscU and facilitates cluster transfer from IscU to recipient apo-proteins. Here we report that the otherwise essential roles of HscA and HscB can be bypassed in vivo by a number of single amino acid substitutions in IscU. CD spectroscopic studies of the variant IscU proteins capable of this bypass activity revealed dynamic interconversion between two conformations: the denatured (D) and the structured (S) state in the absence and presence of Zn<sup>2+</sup> , respectively, which was far more prominent than interconversion observed in wild-type IscU. Furthermore, we found that neither the S-shifted (more structured) variants of IscU nor the perpetually denatured variants could perform their in vivo role regardless of whether the chaperone system was present or not. The present study thus provides for the first time evidence that an in vivo D-state of IscU exists and implies that conformational interconversion between the S- and D-states of the scaffolding protein is a fundamental requirement for the assembly and transfer of the Fe-S cluster.</AbstractText><CopyrightInformation>This article is protected by copyright. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sato</LastName><ForeName>Sakiko</ForeName><Initials>S</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>Matsushima</LastName><ForeName>Yumeka</ForeName><Initials>Y</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>Kanazawa</LastName><ForeName>Miaki</ForeName><Initials>M</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>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>Fujishiro</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><Identifier Source="ORCID">https://orcid.org/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>Kunichika</LastName><ForeName>Kouhei</ForeName><Initials>K</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>Nakamura</LastName><ForeName>Ryosuke</ForeName><Initials>R</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>Tomioka</LastName><ForeName>Hiroaki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Science Education, Graduate School of Education, Saitama University, 255 Shimo-Okubo, Sakura-ku, Saitama, 338-8570, 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">https://orcid.org/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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>11</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Microbiol</MedlineTA><NlmUniqueID>8712028</NlmUniqueID><ISSNLinking>0950-382X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ISC machinery</Keyword><Keyword MajorTopicYN="N">iron-sulfur cluster</Keyword><Keyword MajorTopicYN="N">iron-sulfur protein</Keyword><Keyword MajorTopicYN="N">post-translational modification</Keyword><Keyword MajorTopicYN="N">protein conformation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>11</Month><Day>17</Day><Hour>17</Hour><Minute>13</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>11</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33202070</ArticleId><ArticleId IdType="doi">10.1111/mmi.14646</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Sato, Sakiko" sort="Sato, Sakiko" uniqKey="Sato S" first="Sakiko" last="Sato">Sakiko Sato</name></noRegion><name sortKey="Fujishiro, Takashi" sort="Fujishiro, Takashi" uniqKey="Fujishiro T" first="Takashi" last="Fujishiro">Takashi Fujishiro</name><name sortKey="Kanazawa, Miaki" sort="Kanazawa, Miaki" uniqKey="Kanazawa M" first="Miaki" last="Kanazawa">Miaki Kanazawa</name><name sortKey="Kunichika, Kouhei" sort="Kunichika, Kouhei" uniqKey="Kunichika K" first="Kouhei" last="Kunichika">Kouhei Kunichika</name><name sortKey="Matsushima, Yumeka" sort="Matsushima, Yumeka" uniqKey="Matsushima Y" first="Yumeka" last="Matsushima">Yumeka Matsushima</name><name sortKey="Nakamura, Ryosuke" sort="Nakamura, Ryosuke" uniqKey="Nakamura R" first="Ryosuke" last="Nakamura">Ryosuke Nakamura</name><name sortKey="Takahashi, Yasuhiro" sort="Takahashi, Yasuhiro" uniqKey="Takahashi Y" first="Yasuhiro" last="Takahashi">Yasuhiro Takahashi</name><name sortKey="Tanaka, Naoyuki" sort="Tanaka, Naoyuki" uniqKey="Tanaka N" first="Naoyuki" last="Tanaka">Naoyuki Tanaka</name><name sortKey="Tomioka, Hiroaki" sort="Tomioka, Hiroaki" uniqKey="Tomioka H" first="Hiroaki" last="Tomioka">Hiroaki Tomioka</name><name sortKey="Wada, Kei" sort="Wada, Kei" uniqKey="Wada K" first="Kei" last="Wada">Kei Wada</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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