MersV1, Main, Exploration, bibRecord, 003C24

Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.

Identifieur interne : 003C24 ( Main/Exploration ); précédent : 003C23; suivant : 003C25

Effects 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. Arosio

Source :

The Biochemical journal [ 0264-6021 ] ; 1997.

RBID : pubmed:9065764

Descripteurs français

KwdFr :
- Conformation des protéines, Cystéine (), Dichroïsme circulaire, Dimérisation, Dénaturation des protéines, Ferritines (), Humains, Modèles moléculaires, Mutagenèse dirigée, Mutation, Pliage des protéines, Urée (pharmacologie).
MESH :
- pharmacologie : Urée.
- Conformation des protéines, Cystéine, Dichroïsme circulaire, Dimérisation, Dénaturation des protéines, Ferritines, Humains, Modèles moléculaires, Mutagenèse dirigée, Mutation, Pliage des protéines.

English descriptors

KwdEn :
- Circular Dichroism, Cysteine (chemistry), Dimerization, Ferritins (chemistry), Ferritins (drug effects), Humans, Models, Molecular, Mutagenesis, Site-Directed, Mutation, Protein Conformation, Protein Denaturation, Protein Folding, Urea (pharmacology).
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

Affiliations:

Italie

Le document en format XML

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<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>
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<term>Dénaturation des protéines</term>
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<term>Humains</term>
<term>Modèles moléculaires</term>
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<term>Mutation</term>
<term>Pliage des protéines</term>
<term>Urée (pharmacologie)</term>
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<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>
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<term>Dichroïsme circulaire</term>
<term>Dimérisation</term>
<term>Dénaturation des protéines</term>
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<term>Humains</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Mutation</term>
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<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>
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Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.

Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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