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  • Title: Conversion of ATP-actin to ADP-actin reverses the affinity of monomeric actin for Ca2+ vs Mg2+.
    Author: Selden LA, Gershman LC, Kinosian HJ, Estes JE.
    Journal: FEBS Lett; 1987 Jun 08; 217(1):89-93. PubMed ID: 3595846.
    Abstract:
    Monomeric ATP-actin binds Ca2+ 3-4-times more strongly than Mg2+ at pH 8. On conversion of G-ATP-actin to G-ADP-actin, the relative affinity of actin for the divalent cations is reversed, so that Mg2+ is bound 6-times more strongly than Ca2+. The dissociation rate constant of Ca2+ from Ca-ADP-actin is 50-fold higher than that for Ca2+ from Ca-ATP-actin, suggesting that this reversal of divalent cation affinities is due primarily to a higher equilibrium dissociation constant for Ca-ADP-actin. These results demonstrate an interaction between the actin-bound nucleotide and divalent cation or their binding sites.
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