Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.
Identifieur interne : 002735 ( PubMed/Curation ); précédent : 002734; suivant : 002736Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.
Auteurs : P. Santambrogio [Italie] ; P. Pinto ; S. Levi ; A. Cozzi ; E. Rovida ; A. Albertini ; P. Artymiuk ; P M Harrison ; P. ArosioSource :
- The Biochemical journal [ 0264-6021 ] ; 1997.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Cysteine, Ferritins.
- chemical , drug effects : Ferritins.
- chemical , pharmacology : Urea.
- Circular Dichroism, Dimerization, Humans, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Protein Conformation, Protein Denaturation, Protein Folding.
Abstract
Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus (delta(1-13)), near the 4-fold axis (Leu-169 --> Arg), the 3-fold axis (Asp-131 --> Ile + Glu-134 --> Phe) or the 2-fold axis (Ile-85 --> Cys). We also carried out specific chemical modifications of Cys-130 (near the 3-fold axis) and Cys-85 (near the 2-fold axis). Renaturation of the modified ferritins yielded assembly intermediates that differed in size and physical properties. Alterations of residues around the 2-, 4- and 3-fold axes produced subunit monomers, dimers and higher oligomers respectively. All these intermediates could be induced to assemble into ferritin 24-mers by concentrating them or by co-renaturing them with wild-type H-ferritin. The results support the hypothesis that the symmetric subunit dimers are the building blocks of ferritin assembly, and are consistent with a reassembly pathway involving the coalescence of dimers, probably around the 4-fold axis, followed by stepwise addition of dimers until the 24-mer cage is completed. In addition they show that assembly interactions are responsible for the large hysteresis of folding and unfolding plots. The implications of the studies for in vivo heteropolymer formation in vertebrates, which have two types of ferritin chain (H and L), are discussed.
DOI: 10.1042/bj3220461
PubMed: 9065764
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Cozzi</name></author><author><name sortKey="Rovida, E" sort="Rovida, E" uniqKey="Rovida E" first="E" last="Rovida">E. Rovida</name></author><author><name sortKey="Albertini, A" sort="Albertini, A" uniqKey="Albertini A" first="A" last="Albertini">A. Albertini</name></author><author><name sortKey="Artymiuk, P" sort="Artymiuk, P" uniqKey="Artymiuk P" first="P" last="Artymiuk">P. Artymiuk</name></author><author><name sortKey="Harrison, P M" sort="Harrison, P M" uniqKey="Harrison P" first="P M" last="Harrison">P M Harrison</name></author><author><name sortKey="Arosio, P" sort="Arosio, P" uniqKey="Arosio P" first="P" last="Arosio">P. 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Santambrogio</name><affiliation wicri:level="1"><nlm:affiliation>DIBIT, San Raffaele Scientific Institute, Milano, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>DIBIT, San Raffaele Scientific Institute, Milano</wicri:regionArea></affiliation></author><author><name sortKey="Pinto, P" sort="Pinto, P" uniqKey="Pinto P" first="P" last="Pinto">P. Pinto</name></author><author><name sortKey="Levi, S" sort="Levi, S" uniqKey="Levi S" first="S" last="Levi">S. Levi</name></author><author><name sortKey="Cozzi, A" sort="Cozzi, A" uniqKey="Cozzi A" first="A" last="Cozzi">A. Cozzi</name></author><author><name sortKey="Rovida, E" sort="Rovida, E" uniqKey="Rovida E" first="E" last="Rovida">E. Rovida</name></author><author><name sortKey="Albertini, A" sort="Albertini, A" uniqKey="Albertini A" first="A" last="Albertini">A. Albertini</name></author><author><name sortKey="Artymiuk, P" sort="Artymiuk, P" uniqKey="Artymiuk P" first="P" last="Artymiuk">P. Artymiuk</name></author><author><name sortKey="Harrison, P M" sort="Harrison, P M" uniqKey="Harrison P" first="P M" last="Harrison">P M Harrison</name></author><author><name sortKey="Arosio, P" sort="Arosio, P" uniqKey="Arosio P" first="P" last="Arosio">P. Arosio</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Circular Dichroism</term><term>Cysteine (chemistry)</term><term>Dimerization</term><term>Ferritins (chemistry)</term><term>Ferritins (drug effects)</term><term>Humans</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Urea (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term><term>Cystéine ()</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Dénaturation des protéines</term><term>Ferritines ()</term><term>Humains</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Mutation</term><term>Pliage des protéines</term><term>Urée (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Ferritins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Ferritins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Urea</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Urée</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Dimerization</term><term>Humans</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Mutation</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Folding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cystéine</term><term>Dichroïsme circulaire</term><term>Dimérisation</term><term>Dénaturation des protéines</term><term>Ferritines</term><term>Humains</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Mutation</term><term>Pliage des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus (delta(1-13)), near the 4-fold axis (Leu-169 --> Arg), the 3-fold axis (Asp-131 --> Ile + Glu-134 --> Phe) or the 2-fold axis (Ile-85 --> Cys). We also carried out specific chemical modifications of Cys-130 (near the 3-fold axis) and Cys-85 (near the 2-fold axis). Renaturation of the modified ferritins yielded assembly intermediates that differed in size and physical properties. Alterations of residues around the 2-, 4- and 3-fold axes produced subunit monomers, dimers and higher oligomers respectively. All these intermediates could be induced to assemble into ferritin 24-mers by concentrating them or by co-renaturing them with wild-type H-ferritin. The results support the hypothesis that the symmetric subunit dimers are the building blocks of ferritin assembly, and are consistent with a reassembly pathway involving the coalescence of dimers, probably around the 4-fold axis, followed by stepwise addition of dimers until the 24-mer cage is completed. In addition they show that assembly interactions are responsible for the large hysteresis of folding and unfolding plots. The implications of the studies for in vivo heteropolymer formation in vertebrates, which have two types of ferritin chain (H and L), are discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9065764</PMID><DateCompleted><Year>1997</Year><Month>04</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>322 ( Pt 2)</Volume><PubDate><Year>1997</Year><Month>Mar</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem. J.</ISOAbbreviation></Journal><ArticleTitle>Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.</ArticleTitle><Pagination><MedlinePgn>461-8</MedlinePgn></Pagination><Abstract><AbstractText>Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus (delta(1-13)), near the 4-fold axis (Leu-169 --> Arg), the 3-fold axis (Asp-131 --> Ile + Glu-134 --> Phe) or the 2-fold axis (Ile-85 --> Cys). We also carried out specific chemical modifications of Cys-130 (near the 3-fold axis) and Cys-85 (near the 2-fold axis). Renaturation of the modified ferritins yielded assembly intermediates that differed in size and physical properties. Alterations of residues around the 2-, 4- and 3-fold axes produced subunit monomers, dimers and higher oligomers respectively. All these intermediates could be induced to assemble into ferritin 24-mers by concentrating them or by co-renaturing them with wild-type H-ferritin. The results support the hypothesis that the symmetric subunit dimers are the building blocks of ferritin assembly, and are consistent with a reassembly pathway involving the coalescence of dimers, probably around the 4-fold axis, followed by stepwise addition of dimers until the 24-mer cage is completed. In addition they show that assembly interactions are responsible for the large hysteresis of folding and unfolding plots. The implications of the studies for in vivo heteropolymer formation in vertebrates, which have two types of ferritin chain (H and L), are discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Santambrogio</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>DIBIT, San Raffaele Scientific Institute, Milano, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pinto</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Levi</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Cozzi</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Rovida</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Albertini</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Artymiuk</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Harrison</LastName><ForeName>P M</ForeName><Initials>PM</Initials></Author><Author ValidYN="Y"><LastName>Arosio</LastName><ForeName>P</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>8W8T17847W</RegistryNumber><NameOfSubstance UI="D014508">Urea</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-73-2</RegistryNumber><NameOfSubstance 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