Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions.
Identifieur interne : 001282 ( Main/Exploration ); précédent : 001281; suivant : 001283Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions.
Auteurs : Daisuke Sato [Japon] ; Satsuki Takebe [Japon] ; Atsushi Kurobe [Japon] ; Hideaki Ohtomo [Japon] ; Kazuo Fujiwara [Japon] ; Masamichi Ikeguchi [Japon]Source :
- Biochemistry [ 1520-4995 ] ; 2016.
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène, Concentration osmolaire, Conformation des protéines, Diffusion aux petits angles, Ferritines (), Ferritines (génétique), Ions, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines Escherichia coli (), Protéines Escherichia coli (génétique), Rayons X, Sous-unités de protéines (), Électricité statique.
- MESH :
- génétique : Ferritines, Protéines Escherichia coli.
- Concentration en ions d'hydrogène, Concentration osmolaire, Conformation des protéines, Diffusion aux petits angles, Ferritines, Ions, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines Escherichia coli, Rayons X, Sous-unités de protéines, Électricité statique.
English descriptors
- KwdEn :
- Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Ferritins (chemistry), Ferritins (genetics), Hydrogen-Ion Concentration, Ions, Models, Molecular, Mutation, Osmolar Concentration, Protein Conformation, Protein Multimerization, Protein Subunits (chemistry), Scattering, Small Angle, Static Electricity, X-Rays.
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Ferritins, Protein Subunits.
- chemical , genetics : Escherichia coli Proteins, Ferritins.
- Hydrogen-Ion Concentration, Ions, Models, Molecular, Mutation, Osmolar Concentration, Protein Conformation, Protein Multimerization, Scattering, Small Angle, Static Electricity, X-Rays.
Abstract
Escherichia coli non-heme-binding ferritin A (EcFtnA) is a spherical cagelike protein that is composed of 24 identical subunits. EcFtnA dissociates into 2-mers under acidic conditions and can reassemble into the native structure when the pH is increased. To understand how electrostatic interactions influence the assembly reaction, the dependence of the process on ionic strength and pH was investigated. The assembly reaction was initiated by stopped-flow mixing of the acid-dissociated EcFtnA solution and high-pH buffer solutions and monitored by time-resolved small-angle X-ray scattering. The rate of assembly increased with increasing ionic strength and decreased with increasing pH from 6 to 8. These dependences were thought to originate from repulsion between assembly units (2-mer in the case of EcFtnA) with the same net charge sign; therefore, to test this assumption, mutants with different net charges (net-charge mutants) were prepared. In buffers with a low ionic strength, the rate of assembly increased with a decreasing net charge. Thus, repulsion between the assembly unit net charges was demonstrated to be an important factor determining the rate of assembly. However, the difference in the assembly rate among net-charge mutants was not significant in buffers with an ionic strength of >0.1. Notably, under such high-ionic strength conditions, the assembly rate increased with an increasing ionic strength, suggesting that local electrostatic interactions are also responsible for the ionic strength dependence of the rate of assembly and are repulsive on average.
DOI: 10.1021/acs.biochem.5b01197
PubMed: 26716350
Affiliations:
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192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kurobe, Atsushi" sort="Kurobe, Atsushi" uniqKey="Kurobe A" first="Atsushi" last="Kurobe">Atsushi Kurobe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Ohtomo, Hideaki" sort="Ohtomo, Hideaki" 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Daisuke" uniqKey="Sato D" first="Daisuke" last="Sato">Daisuke Sato</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Takebe, Satsuki" sort="Takebe, Satsuki" uniqKey="Takebe S" first="Satsuki" last="Takebe">Satsuki Takebe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Kurobe, Atsushi" sort="Kurobe, Atsushi" uniqKey="Kurobe A" first="Atsushi" last="Kurobe">Atsushi Kurobe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Ohtomo, Hideaki" sort="Ohtomo, Hideaki" uniqKey="Ohtomo H" first="Hideaki" last="Ohtomo">Hideaki Ohtomo</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Fujiwara, Kazuo" sort="Fujiwara, Kazuo" uniqKey="Fujiwara K" first="Kazuo" last="Fujiwara">Kazuo Fujiwara</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Ikeguchi, Masamichi" sort="Ikeguchi, Masamichi" uniqKey="Ikeguchi M" first="Masamichi" last="Ikeguchi">Masamichi Ikeguchi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Bioinformatics, Soka University , 1-236 Tangi-machi, Hachioji, Tokyo 192-8577</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Escherichia coli Proteins (chemistry)</term><term>Escherichia coli Proteins (genetics)</term><term>Ferritins (chemistry)</term><term>Ferritins (genetics)</term><term>Hydrogen-Ion Concentration</term><term>Ions</term><term>Models, Molecular</term><term>Mutation</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Protein Subunits (chemistry)</term><term>Scattering, Small Angle</term><term>Static Electricity</term><term>X-Rays</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Diffusion aux petits angles</term><term>Ferritines ()</term><term>Ferritines (génétique)</term><term>Ions</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Protéines Escherichia coli ()</term><term>Protéines Escherichia coli (génétique)</term><term>Rayons X</term><term>Sous-unités de protéines ()</term><term>Électricité statique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term><term>Ferritins</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Escherichia coli Proteins</term><term>Ferritins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferritines</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Ions</term><term>Models, Molecular</term><term>Mutation</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Scattering, Small Angle</term><term>Static Electricity</term><term>X-Rays</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Diffusion aux petits angles</term><term>Ferritines</term><term>Ions</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Protéines Escherichia coli</term><term>Rayons X</term><term>Sous-unités de protéines</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Escherichia coli non-heme-binding ferritin A (EcFtnA) is a spherical cagelike protein that is composed of 24 identical subunits. EcFtnA dissociates into 2-mers under acidic conditions and can reassemble into the native structure when the pH is increased. To understand how electrostatic interactions influence the assembly reaction, the dependence of the process on ionic strength and pH was investigated. The assembly reaction was initiated by stopped-flow mixing of the acid-dissociated EcFtnA solution and high-pH buffer solutions and monitored by time-resolved small-angle X-ray scattering. The rate of assembly increased with increasing ionic strength and decreased with increasing pH from 6 to 8. These dependences were thought to originate from repulsion between assembly units (2-mer in the case of EcFtnA) with the same net charge sign; therefore, to test this assumption, mutants with different net charges (net-charge mutants) were prepared. In buffers with a low ionic strength, the rate of assembly increased with a decreasing net charge. Thus, repulsion between the assembly unit net charges was demonstrated to be an important factor determining the rate of assembly. However, the difference in the assembly rate among net-charge mutants was not significant in buffers with an ionic strength of >0.1. Notably, under such high-ionic strength conditions, the assembly rate increased with an increasing ionic strength, suggesting that local electrostatic interactions are also responsible for the ionic strength dependence of the rate of assembly and are repulsive on average. </div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Sato, Daisuke" sort="Sato, Daisuke" uniqKey="Sato D" first="Daisuke" last="Sato">Daisuke Sato</name></region><name sortKey="Fujiwara, Kazuo" sort="Fujiwara, Kazuo" uniqKey="Fujiwara K" first="Kazuo" last="Fujiwara">Kazuo Fujiwara</name><name sortKey="Ikeguchi, Masamichi" sort="Ikeguchi, Masamichi" uniqKey="Ikeguchi M" first="Masamichi" last="Ikeguchi">Masamichi Ikeguchi</name><name sortKey="Kurobe, Atsushi" sort="Kurobe, Atsushi" uniqKey="Kurobe A" first="Atsushi" last="Kurobe">Atsushi Kurobe</name><name sortKey="Ohtomo, Hideaki" sort="Ohtomo, Hideaki" uniqKey="Ohtomo H" first="Hideaki" last="Ohtomo">Hideaki Ohtomo</name><name sortKey="Takebe, Satsuki" sort="Takebe, Satsuki" uniqKey="Takebe S" first="Satsuki" last="Takebe">Satsuki Takebe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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