Calcium-induced conformational changes in the amino-terminal half of gelsolin

Autor: Sutherland K. Maciver, Abdellatif Fattoum, Claude Roustan, Bertrand Rebiere, Imen Ferjani, Yves Benyamin
Přispěvatelé: Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1)
Rok vydání: 2007
Předmět:
MESH: Hydrogen-Ion Concentration
Amino terminal
Apoptosis
Biochemistry
MESH: Protein Structure
Tertiary
Structural Biology
MESH: Peptide Fragments
Dansyl Compounds
0303 health sciences
medicine.diagnostic_test
Chemistry
Actin cytoskeleton
030302 biochemistry & molecular biology
Tryptophan
Hydrogen-Ion Concentration
MESH: Calcium
Calcium-binding
Protein Binding
Proteolysis
Biophysics
chemistry.chemical_element
Context (language use)
macromolecular substances
Buffers
Calcium
MESH: Actins
Fluorescence
03 medical and health sciences
Genetics
medicine
Humans
MESH: Protein Binding
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Molecular Biology
Gelsolin
MESH: Tryptophan
Actin
MESH: Dansyl Compounds
030304 developmental biology
Binding Sites
MESH: Humans
MESH: Fluorescence
Cell Biology
Actins
Peptide Fragments
Protein Structure
Tertiary
MESH: Gelsolin
MESH: Binding Sites
MESH: Buffers
Zdroj: FEBS Letters
FEBS Letters, Wiley, 2007, 581 (4), pp.681-6. ⟨10.1016/j.febslet.2007.01.031⟩
ISSN: 0014-5793
1873-3468
DOI: 10.1016/j.febslet.2007.01.031
Popis: Gelsolin is an actin-binding protein that is regulated by the occupancy of multiple calcium-binding sites. We have studied calcium induced conformational changes in the G1-2 and G1-3 sub-domains, and report the binding affinities for the three type II sites. A new probe for G3 has been produced and a Kd of 5 lM has been measured for calcium in the context of G1-3. The two halves of gelsolin, G1-3 and G4-6 bind weakly with or without calcium, suggesting that once separated by apop- totic proteolysis, G1-3 and G4-6 remain apart allowing G1-3 to sever actin in a calcium free manner. � 2007 Federation of European Biochemical Societies. Pub- lished by Elsevier B.V. All rights reserved.
Databáze: OpenAIRE
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