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Changes in actin lysine reactivities during polymerization detected using a competitive labeling method.

S E Hitchcock-De Gregori, S Mandala, G A Sachs

    The Journal of Biological Chemistry
    |November 10, 1982
    PubMed
    Summary

    We mapped actin structure by measuring lysine reactivity. Polymerization and magnesium ions alter reactivity, revealing potential monomer contact sites in actin filaments.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Protein Chemistry

    Background:

    • Actin is a crucial protein for cell structure and motility.
    • Understanding actin filament formation requires detailed knowledge of its structural dynamics.

    Purpose of the Study:

    • To investigate the structural changes in actin upon polymerization.
    • To identify specific lysine residues involved in actin monomer-protein interactions.

    Main Methods:

    • Competitive labeling using acetic anhydride to measure lysine reactivity.
    • Comparison of monomeric globular actin with polymerized filamentous actin under varying salt and magnesium conditions.

    Main Results:

    • Identified 12 reactive lysine residues in actin.

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  • Lysines 325 and 327 are consistently the most reactive.
  • Polymerization and Mg2+ significantly decrease the reactivity of specific lysines (e.g., 50, 61, 68, 113, 290).
  • Reduced reactivity of certain lysines suggests their involvement in inter-monomer contacts within actin filaments.

    • Conclusions:

    • Actin polymerization involves significant structural rearrangements affecting lysine accessibility.
    • Specific lysine residues, particularly in the N-terminal region, are likely involved in actin filament formation.
    • Magnesium ions play a role in modulating actin structure beyond simple polymerization.