The dimer-tetramer equilibrium of recombinant hemoglobins. Stabilization of the α1β2 interface by the mutation β(Cys112 → Gly) at the α1β1 interface
Identifieur interne : 003868 ( Main/Exploration ); précédent : 003867; suivant : 003869The dimer-tetramer equilibrium of recombinant hemoglobins. Stabilization of the α1β2 interface by the mutation β(Cys112 → Gly) at the α1β1 interface
Auteurs : Clara Fronticelli [États-Unis] ; Maurizio Gattoni [Italie] ; A-Lien Lu [États-Unis] ; William S. Brinigar [États-Unis] ; Jeffries L. G. Bucci [États-Unis] ; Emilia Chiancone [Italie]Source :
- Biophysical Chemistry [ 0301-4622 ] ; 1994.
Abstract
The dimer-tetramer association constants of several recombinant human hemoglobins (in the CO form) have been measured by differential gel filtration. Recombinant human hemoglobin prepared from recombinant β-chains, and mutant hemoglobins where the substitution was on the surface, β(Thr4 → Asp), in the heme pocket, β(Val67 → Thr), at the 2,3-DPG binding site, β(Val1 → Met + His2del), had a twofold smaller association with respect to natural hemoglobin. In a mutant at the α1β21 interface, β(Cys93 → Ala), the association constant was decreased three-fold. Conversely, in a mutant at the α1β1 interface, β(Cys112 → Gly), the association constant was two- and four-fold increased with respect to natural and recombinant human hemoglobin. These differences are energetically very small, consistent with the correct folding of the recombinant hemoglobins. The stabilization of the tetrameric structure by a mutation at the α1β1 interface indicates that structural changes at this interface can be propagated through the protein to the α1β2 interface and, thereby, exert an effect on the allosteric equilibrium.
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DOI: 10.1016/0301-4622(94)00028-X
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Stabilization of the α1β2 interface by the mutation β(Cys112 → Gly) at the α1β1 interface</title><author><name sortKey="Fronticelli, Clara" sort="Fronticelli, Clara" uniqKey="Fronticelli C" first="Clara" last="Fronticelli">Clara Fronticelli</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Maryland, School of Medicine, 108 N. Greene St., Baltimore, MD 21201</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Gattoni, Maurizio" sort="Gattoni, Maurizio" uniqKey="Gattoni M" first="Maurizio" last="Gattoni">Maurizio Gattoni</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>CNR Center for Molecular Biology, Department of Biochemical Sciences A. 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Brinigar</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Temple University, Philadelphia PA 19122</wicri:regionArea><wicri:noRegion>Philadelphia PA 19122</wicri:noRegion></affiliation></author><author><name sortKey="Bucci, Jeffries L G" sort="Bucci, Jeffries L G" uniqKey="Bucci J" first="Jeffries L. G." last="Bucci">Jeffries L. G. Bucci</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, University of Maryland, School of Medicine, 108 N. 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Recombinant human hemoglobin prepared from recombinant β-chains, and mutant hemoglobins where the substitution was on the surface, β(Thr4 → Asp), in the heme pocket, β(Val67 → Thr), at the 2,3-DPG binding site, β(Val1 → Met + His2del), had a twofold smaller association with respect to natural hemoglobin. In a mutant at the α1β21 interface, β(Cys93 → Ala), the association constant was decreased three-fold. Conversely, in a mutant at the α1β1 interface, β(Cys112 → Gly), the association constant was two- and four-fold increased with respect to natural and recombinant human hemoglobin. These differences are energetically very small, consistent with the correct folding of the recombinant hemoglobins. The stabilization of the tetrameric structure by a mutation at the α1β1 interface indicates that structural changes at this interface can be propagated through the protein to the α1β2 interface and, thereby, exert an effect on the allosteric equilibrium.</div></front></TEI><affiliations><list><country><li>Italie</li><li>États-Unis</li></country><region><li>Latium</li><li>Maryland</li></region><settlement><li>Rome</li></settlement></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Fronticelli, Clara" sort="Fronticelli, Clara" uniqKey="Fronticelli C" first="Clara" last="Fronticelli">Clara Fronticelli</name></region><name sortKey="Brinigar, William S" sort="Brinigar, William S" uniqKey="Brinigar W" first="William S." last="Brinigar">William S. Brinigar</name><name sortKey="Bucci, Jeffries L G" sort="Bucci, Jeffries L G" uniqKey="Bucci J" first="Jeffries L. G." last="Bucci">Jeffries L. G. Bucci</name><name sortKey="Lu, A Lien" sort="Lu, A Lien" uniqKey="Lu A" first="A-Lien" last="Lu">A-Lien Lu</name></country><country name="Italie"><region name="Latium"><name sortKey="Gattoni, Maurizio" sort="Gattoni, Maurizio" uniqKey="Gattoni M" first="Maurizio" last="Gattoni">Maurizio Gattoni</name></region><name sortKey="Chiancone, Emilia" sort="Chiancone, Emilia" uniqKey="Chiancone E" first="Emilia" last="Chiancone">Emilia Chiancone</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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