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Interaction of G-actin with thymosin β4 and its variants thymosin β9 and thymosin β met9

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Summary

Thymosin β4 is a major actin sequestering peptide in vertebrate cells and plays a role in the regulation of actin monomer/polymer ratio. Thymosin β9 and thymosin β met9 are minor variants of thymosin β4. The possible function of these peptides has been investigated by comparing the actin binding properties of these β-thymosins. Thymosin β9 and thymosin β met9 were found to inhibit polymerization of ATP-actin with identical K d s of 0.7–0.8 μM (as compared to 2±0.3 μM for thymosin β4); like thymosin β4, they bound to ADP-G-actin with a 100-fold lower affinity than to ATP-G-actin. The interaction of thymosin β4 and thymosin β met9 with G-actin was weakened 20-fold upon oxidation of methionine-6 into methionine sulfoxide. Binding of thymosin β4 to G-actin was accompanied by a 15% increase in the fluorescence intensity of actin tryptophans, and a 10 nm emission blue shift. Methionine-6 played an important role in this effect. The fluorescence change was used to monitor the kinetics of thymosin β4 binding to G-actin in the stopped-flow. The reaction was bimolecular, with association and dissociation rate constants of ∼1.5 μM-1 s-1 and 2s-1 respectively, under physiological conditions. The possible physiological significances of methionine-6 oxidation and of the relatively slow binding kinetics in regulating thymosin β4 function in vivo is discussed.

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Authors and Affiliations

  1. Laboratoire d'Enzymologie, CNRS, 91198, Gif-sur-Yvette, France

    Catherine Jean, Laurent Blanchoin, Marie-France Carlier & Dominique Pantaloni

  2. Institut de Chimie des Substances Naturelles, CNRS, 91198, Gif-sur-Yvette, France

    Klaus Rieger & Maryse Lenfant

Authors
  1. Catherine Jean
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  2. Klaus Rieger
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  3. Laurent Blanchoin
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  4. Marie-France Carlier
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  5. Maryse Lenfant
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  6. Dominique Pantaloni
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Jean, C., Rieger, K., Blanchoin, L. et al. Interaction of G-actin with thymosin β4 and its variants thymosin β9 and thymosin β met9 . J Muscle Res Cell Motil 15, 278–286 (1994). https://doi.org/10.1007/BF00123480

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  • DOI: https://doi.org/10.1007/BF00123480

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