MersV1, PubMed, Checkpoint, bibRecord, 002693

Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin.

Identifieur interne : 002693 ( PubMed/Checkpoint ); précédent : 002692; suivant : 002694

Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin.

Auteurs : O. Van Wuytswinkel [France] ; J F Briat

Source :

The Biochemical journal [ 0264-6021 ] ; 1995.

RBID : pubmed:7848297

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Base Sequence, Ferritins (chemistry), Ferritins (genetics), Molecular Sequence Data, Mutagenesis, Site-Directed, Peas, Peptide Fragments (chemistry), Plant Proteins (chemistry), Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Recombinant Proteins (chemistry), Seeds (chemistry), Structure-Activity Relationship, Thermodynamics, Urea.
MESH :
- chemical , chemistry : Ferritins, Peptide Fragments, Plant Proteins, Recombinant Proteins.
- chemical , genetics : Ferritins.
- chemistry : Seeds.
- Amino Acid Sequence, Base Sequence, Molecular Sequence Data, Mutagenesis, Site-Directed, Peas, Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Structure-Activity Relationship, Thermodynamics, Urea.

Abstract

Plant ferritin has a three-dimensional structure predicted to be very similar to that of animal ferritin. It has, however, an additional specific sequence of 24 amino acids at its N-terminus named extension peptide (EP). In order to determine precisely the interactions between EP and other domains of the pea seed ferritin subunit, three point mutations were performed. The mutated residues were chosen by three-dimensional computer modelling of the pea seed ferritin subunit structure [Lobréaux, Yewdall, Briat and Harrison (1992) Biochem. J. 228, 931-939]. The mutant recombinant proteins were expressed in Escherichia coli and purified to homogeneity; all the mutants were found to be assembled as 24-mers. When Ala-13 was replaced by His, as in mammalian ferritins, ferroxidase activity was significantly reduced. Moreover, in vitro iron-core formation in Pro-X-->Ala, Lys-R-->Glu and Ala-13-->His mutants was increased after denaturation by urea followed by renaturation; this was also observed with the EP deletion mutant (r delta TP/EP). The recombinant ferritins were also analysed using tryptophan fluorescence spectra. The r delta TP/EP, Pro-X-->Ala and Lys-R-->Glu mutants were found to be more susceptible to denaturation by urea than the native r delta TP pea seed ferritin.

DOI: 10.1042/bj3050959
PubMed: 7848297

Affiliations:

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Le document en format XML

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<term>Base Sequence</term>
<term>Ferritins (chemistry)</term>
<term>Ferritins (genetics)</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Peas</term>
<term>Peptide Fragments (chemistry)</term>
<term>Plant Proteins (chemistry)</term>
<term>Protein Conformation</term>
<term>Protein Denaturation</term>
<term>Protein Structure, Secondary</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Seeds (chemistry)</term>
<term>Structure-Activity Relationship</term>
<term>Thermodynamics</term>
<term>Urea</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines</term>
<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Ferritines ()</term>
<term>Ferritines (génétique)</term>
<term>Fragments peptidiques ()</term>
<term>Graines ()</term>
<term>Mutagenèse dirigée</term>
<term>Pois</term>
<term>Protéines recombinantes ()</term>
<term>Protéines végétales ()</term>
<term>Relation structure-activité</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Thermodynamique</term>
<term>Urée</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ferritins</term>
<term>Peptide Fragments</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ferritins</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Seeds</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferritines</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Peas</term>
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<term>Protein Denaturation</term>
<term>Protein Structure, Secondary</term>
<term>Structure-Activity Relationship</term>
<term>Thermodynamics</term>
<term>Urea</term>
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<term>Données de séquences moléculaires</term>
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<term>Fragments peptidiques</term>
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<term>Protéines végétales</term>
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<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
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<front><div type="abstract" xml:lang="en">Plant ferritin has a three-dimensional structure predicted to be very similar to that of animal ferritin. It has, however, an additional specific sequence of 24 amino acids at its N-terminus named extension peptide (EP). In order to determine precisely the interactions between EP and other domains of the pea seed ferritin subunit, three point mutations were performed. The mutated residues were chosen by three-dimensional computer modelling of the pea seed ferritin subunit structure [Lobréaux, Yewdall, Briat and Harrison (1992) Biochem. J. 228, 931-939]. The mutant recombinant proteins were expressed in Escherichia coli and purified to homogeneity; all the mutants were found to be assembled as 24-mers. When Ala-13 was replaced by His, as in mammalian ferritins, ferroxidase activity was significantly reduced. Moreover, in vitro iron-core formation in Pro-X-->Ala, Lys-R-->Glu and Ala-13-->His mutants was increased after denaturation by urea followed by renaturation; this was also observed with the EP deletion mutant (r delta TP/EP). The recombinant ferritins were also analysed using tryptophan fluorescence spectra. The r delta TP/EP, Pro-X-->Ala and Lys-R-->Glu mutants were found to be more susceptible to denaturation by urea than the native r delta TP pea seed ferritin.</div>
</front>
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<Abstract><AbstractText>Plant ferritin has a three-dimensional structure predicted to be very similar to that of animal ferritin. It has, however, an additional specific sequence of 24 amino acids at its N-terminus named extension peptide (EP). In order to determine precisely the interactions between EP and other domains of the pea seed ferritin subunit, three point mutations were performed. The mutated residues were chosen by three-dimensional computer modelling of the pea seed ferritin subunit structure [Lobréaux, Yewdall, Briat and Harrison (1992) Biochem. J. 228, 931-939]. The mutant recombinant proteins were expressed in Escherichia coli and purified to homogeneity; all the mutants were found to be assembled as 24-mers. When Ala-13 was replaced by His, as in mammalian ferritins, ferroxidase activity was significantly reduced. Moreover, in vitro iron-core formation in Pro-X-->Ala, Lys-R-->Glu and Ala-13-->His mutants was increased after denaturation by urea followed by renaturation; this was also observed with the EP deletion mutant (r delta TP/EP). The recombinant ferritins were also analysed using tryptophan fluorescence spectra. The r delta TP/EP, Pro-X-->Ala and Lys-R-->Glu mutants were found to be more susceptible to denaturation by urea than the native r delta TP pea seed ferritin.</AbstractText>
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Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin.

Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin.

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