Interaction of F-actin with phosphate analogues studied by differential scanning calorimetry

Interaction of F-actin with phosphate analogues studied by differential scanning calorimetry

The thermal unfolding of F-actin and the changes induced in it by the binding of phosphate analogues were studied by differential scanning calorimetry. It is shown that the conformation of actin is drastically altered by interaction with beryllium fluoride or aluminium fluoride, while the effects of...

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Bibliographic Details
Published in:FEBS letters Vol. 351; no. 1; pp. 15 - 18
Main Authors: Nikolaeva, Olga P., Dedova, Irina V., Khvorova, Irina S., Levitsky, Dmitrii I.
Format: Journal Article
Language:English
Published: England Elsevier B.V 29-08-1994
Subjects:
Actins - metabolism
Aluminium fluoride
Aluminum Compounds - metabolism
Animals
Beryllium - metabolism
Beryllium fluoride
Binding Sites
Calorimetry, Differential Scanning
Differential scanning calorimetry
F-actin
Fluorides - metabolism
Phosphates - metabolism
Protein Conformation
Protein Denaturation
Rabbits
Beryllium fluoride
Differential scanning calorimetry
Aluminium fluoride
F-actin
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Summary:The thermal unfolding of F-actin and the changes induced in it by the binding of phosphate analogues were studied by differential scanning calorimetry. It is shown that the conformation of actin is drastically altered by interaction with beryllium fluoride or aluminium fluoride, while the effects of vanadate and phosphate are negligible. The effect of beryllium fluoride on the F-actin structure, as reflected in a significant increase of the actin thermal stability, is much more pronounced in the presence of Mg 2+ than in the case of F-actin polymerized by KCl or LiCl in the absence of Mg 2+. It is concluded that differential scanning calorimetry is a very convenient method for probing the conformational changes in F-actin caused by the interaction with phosphate analogues.
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content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(94)00801-9