Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.
Identifieur interne : 000170 ( Main/Exploration ); précédent : 000169; suivant : 000171Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.
Auteurs : Malgorzata Kleczewska [Pologne] ; Aneta Grabinska [Pologne] ; Marcin Jelen [Pologne] ; Milena Stolarska [Pologne] ; Brenda Schilke [États-Unis] ; Jaroslaw Marszalek [Pologne, États-Unis] ; Elizabeth A. Craig [États-Unis] ; Rafal Dutkiewicz [Pologne]Source :
- International journal of molecular sciences [ 1422-0067 ] ; 2020.
Abstract
Mitochondria play a central role in the biogenesis of iron-sulfur cluster(s) (FeS), protein cofactors needed for many cellular activities. After assembly on scaffold protein Isu, the cluster is transferred onto a recipient apo-protein. Transfer requires Isu interaction with an Hsp70 chaperone system that includes a dedicated J-domain protein co-chaperone (Hsc20). Hsc20 stimulates Hsp70's ATPase activity, thus stabilizing the critical Isu-Hsp70 interaction. While most eukaryotes utilize a multifunctional mitochondrial (mt)Hsp70, yeast employ another Hsp70 (Ssq1), a product of mtHsp70 gene duplication. Ssq1 became specialized in FeS biogenesis, recapitulating the process in bacteria, where specialized Hsp70 HscA cooperates exclusively with an ortholog of Hsc20. While it is well established that Ssq1 and HscA converged functionally for FeS transfer, whether these two Hsp70s possess similar biochemical properties was not known. Here, we show that overall HscA and Ssq1 biochemical properties are very similar, despite subtle differences being apparent - the ATPase activity of HscA is stimulated to a somewhat higher levels by Isu and Hsc20, while Ssq1 has a higher affinity for Isu and for Hsc20. HscA/Ssq1 are a unique example of biochemical convergence of distantly related Hsp70s, with practical implications, crossover experimental results can be combined, facilitating understanding of the FeS transfer process.
DOI: 10.3390/ijms21093326
PubMed: 32397253
PubMed Central: PMC7247549
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Poland.</nlm:affiliation><country xml:lang="fr">Pologne</country><wicri:regionArea>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk</wicri:regionArea><wicri:noRegion>80-307 Gdansk</wicri:noRegion></affiliation></author><author><name sortKey="Schilke, Brenda" sort="Schilke, Brenda" uniqKey="Schilke B" first="Brenda" last="Schilke">Brenda Schilke</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706</wicri:regionArea><placeName><region type="state">Wisconsin</region></placeName></affiliation></author><author><name sortKey="Marszalek, Jaroslaw" sort="Marszalek, Jaroslaw" uniqKey="Marszalek J" first="Jaroslaw" last="Marszalek">Jaroslaw Marszalek</name><affiliation wicri:level="1"><nlm:affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</nlm:affiliation><country xml:lang="fr">Pologne</country><wicri:regionArea>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk</wicri:regionArea><wicri:noRegion>80-307 Gdansk</wicri:noRegion></affiliation><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706</wicri:regionArea><placeName><region type="state">Wisconsin</region></placeName></affiliation></author><author><name sortKey="Craig, Elizabeth A" sort="Craig, Elizabeth A" uniqKey="Craig E" first="Elizabeth A" last="Craig">Elizabeth A. Craig</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706</wicri:regionArea><placeName><region type="state">Wisconsin</region></placeName></affiliation></author><author><name sortKey="Dutkiewicz, Rafal" sort="Dutkiewicz, Rafal" uniqKey="Dutkiewicz R" first="Rafal" last="Dutkiewicz">Rafal Dutkiewicz</name><affiliation wicri:level="1"><nlm:affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</nlm:affiliation><country xml:lang="fr">Pologne</country><wicri:regionArea>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk</wicri:regionArea><wicri:noRegion>80-307 Gdansk</wicri:noRegion></affiliation></author></analytic><series><title level="j">International journal of molecular sciences</title><idno type="eISSN">1422-0067</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">Mitochondria play a central role in the biogenesis of iron-sulfur cluster(s) (FeS), protein cofactors needed for many cellular activities. After assembly on scaffold protein Isu, the cluster is transferred onto a recipient apo-protein. Transfer requires Isu interaction with an Hsp70 chaperone system that includes a dedicated J-domain protein co-chaperone (Hsc20). Hsc20 stimulates Hsp70's ATPase activity, thus stabilizing the critical Isu-Hsp70 interaction. While most eukaryotes utilize a multifunctional mitochondrial (mt)Hsp70, yeast employ another Hsp70 (Ssq1), a product of mtHsp70 gene duplication. Ssq1 became specialized in FeS biogenesis, recapitulating the process in bacteria, where specialized Hsp70 HscA cooperates exclusively with an ortholog of Hsc20. While it is well established that Ssq1 and HscA converged functionally for FeS transfer, whether these two Hsp70s possess similar biochemical properties was not known. Here, we show that overall HscA and Ssq1 biochemical properties are very similar, despite subtle differences being apparent - the ATPase activity of HscA is stimulated to a somewhat higher levels by Isu and Hsc20, while Ssq1 has a higher affinity for Isu and for Hsc20. HscA/Ssq1 are a unique example of biochemical convergence of distantly related Hsp70s, with practical implications, crossover experimental results can be combined, facilitating understanding of the FeS transfer process.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32397253</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1422-0067</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>9</Issue><PubDate><Year>2020</Year><Month>May</Month><Day>08</Day></PubDate></JournalIssue><Title>International journal of molecular sciences</Title><ISOAbbreviation>Int J Mol Sci</ISOAbbreviation></Journal><ArticleTitle>Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E3326</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/ijms21093326</ELocationID><Abstract><AbstractText>Mitochondria play a central role in the biogenesis of iron-sulfur cluster(s) (FeS), protein cofactors needed for many cellular activities. After assembly on scaffold protein Isu, the cluster is transferred onto a recipient apo-protein. Transfer requires Isu interaction with an Hsp70 chaperone system that includes a dedicated J-domain protein co-chaperone (Hsc20). Hsc20 stimulates Hsp70's ATPase activity, thus stabilizing the critical Isu-Hsp70 interaction. While most eukaryotes utilize a multifunctional mitochondrial (mt)Hsp70, yeast employ another Hsp70 (Ssq1), a product of mtHsp70 gene duplication. Ssq1 became specialized in FeS biogenesis, recapitulating the process in bacteria, where specialized Hsp70 HscA cooperates exclusively with an ortholog of Hsc20. While it is well established that Ssq1 and HscA converged functionally for FeS transfer, whether these two Hsp70s possess similar biochemical properties was not known. Here, we show that overall HscA and Ssq1 biochemical properties are very similar, despite subtle differences being apparent - the ATPase activity of HscA is stimulated to a somewhat higher levels by Isu and Hsc20, while Ssq1 has a higher affinity for Isu and for Hsc20. HscA/Ssq1 are a unique example of biochemical convergence of distantly related Hsp70s, with practical implications, crossover experimental results can be combined, facilitating understanding of the FeS transfer process.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kleczewska</LastName><ForeName>Malgorzata</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0002-8580-8767</Identifier><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grabinska</LastName><ForeName>Aneta</ForeName><Initials>A</Initials><Identifier Source="ORCID">0000-0002-3817-4562</Identifier><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jelen</LastName><ForeName>Marcin</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stolarska</LastName><ForeName>Milena</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0002-9428-4213</Identifier><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schilke</LastName><ForeName>Brenda</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marszalek</LastName><ForeName>Jaroslaw</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-6978-1189</Identifier><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Craig</LastName><ForeName>Elizabeth A</ForeName><Initials>EA</Initials><Identifier Source="ORCID">0000-0002-9381-4307</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, WI 53706, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dutkiewicz</LastName><ForeName>Rafal</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0003-4150-0450</Identifier><AffiliationInfo><Affiliation>Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307 Gdansk, Poland.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R35 GM127009</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>UMO-2015/19/B/NZ1/00237</GrantID><Agency>Narodowe Centrum Nauki</Agency><Country></Country></Grant><Grant><GrantID>TEAM POIR.04.04.00-00-4114 /17-00</GrantID><Agency>Fundacja na rzecz Nauki Polskiej</Agency><Country></Country></Grant><Grant><GrantID>R35GM127009</GrantID><Agency>National Institutes of Health</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>05</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Int J Mol Sci</MedlineTA><NlmUniqueID>101092791</NlmUniqueID><ISSNLinking>1422-0067</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">FeS transfer</Keyword><Keyword MajorTopicYN="N">J-domain protein cochaperones</Keyword><Keyword MajorTopicYN="N">gene duplication</Keyword><Keyword MajorTopicYN="N">molecular chaperones</Keyword><Keyword MajorTopicYN="N">protein evolution</Keyword><Keyword MajorTopicYN="N">yeast</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>04</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate 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22;16(16):1660-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16920629</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Pologne</li><li>États-Unis</li></country><region><li>Wisconsin</li></region></list><tree><country name="Pologne"><noRegion><name sortKey="Kleczewska, Malgorzata" sort="Kleczewska, Malgorzata" uniqKey="Kleczewska M" first="Malgorzata" last="Kleczewska">Malgorzata Kleczewska</name></noRegion><name sortKey="Dutkiewicz, Rafal" sort="Dutkiewicz, Rafal" uniqKey="Dutkiewicz R" first="Rafal" last="Dutkiewicz">Rafal Dutkiewicz</name><name sortKey="Grabinska, Aneta" sort="Grabinska, Aneta" uniqKey="Grabinska A" first="Aneta" last="Grabinska">Aneta Grabinska</name><name sortKey="Jelen, Marcin" sort="Jelen, Marcin" uniqKey="Jelen M" first="Marcin" last="Jelen">Marcin Jelen</name><name sortKey="Marszalek, Jaroslaw" sort="Marszalek, Jaroslaw" uniqKey="Marszalek J" first="Jaroslaw" last="Marszalek">Jaroslaw Marszalek</name><name sortKey="Stolarska, Milena" sort="Stolarska, Milena" uniqKey="Stolarska M" first="Milena" last="Stolarska">Milena Stolarska</name></country><country name="États-Unis"><region name="Wisconsin"><name sortKey="Schilke, Brenda" sort="Schilke, Brenda" uniqKey="Schilke B" first="Brenda" last="Schilke">Brenda Schilke</name></region><name sortKey="Craig, Elizabeth A" sort="Craig, Elizabeth A" uniqKey="Craig E" first="Elizabeth A" last="Craig">Elizabeth A. Craig</name><name sortKey="Marszalek, Jaroslaw" sort="Marszalek, Jaroslaw" uniqKey="Marszalek J" first="Jaroslaw" last="Marszalek">Jaroslaw Marszalek</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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