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Water in actin polymerization.

N Fuller1, R P Rand

  • 1Department of Biological Sciences, Brock University, St. Catharines, Ontario, Canada.

Biophysical Journal
|June 4, 1999
PubMed
Summary
This summary is machine-generated.

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Water molecules are released during actin polymerization, particularly in the G-Ca-ATP actin form. Reducing water activity favors actin polymerization, suggesting water originates from the nucleotide binding site cleft.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biophysics

Background:

  • Actin polymerization is crucial for cell structure and motility.
  • The role of water in actin polymerization remains incompletely understood.
  • G-actin transitions to F-actin, forming filaments.

Purpose of the Study:

  • To investigate the involvement of water in the G- to F-actin polymerization reaction.
  • To determine if water is released during actin polymerization.
  • To explore the influence of osmotic stress on actin polymerization dynamics.

Main Methods:

  • Osmotic stress was applied using six different osmolytes.
  • The critical concentration for G-Ca-ATP actin polymerization was measured.
  • Osmotic effects on Mg-ATP actin polymerization were assessed.

Related Experiment Videos

  • Conformational changes in actin nucleotide binding sites were analyzed.

    • Main Results:

    • Reducing water activity significantly lowered the critical concentration for G-Ca-ATP actin.
    • The effect of osmolytes correlated with their molecular weight, suggesting water release.
    • An estimated 10-12 fewer water molecules were associated with polymerized actin.
    • Osmotic effects were negligible for Mg-ATP actin.
    • The Mg-ATP actin conformation is more closed, resembling polymerized actin.

    Conclusions:

    • Water is released during the polymerization of G-Ca-ATP actin.
    • Reduced water activity favors actin polymerization.
    • The nucleotide binding site cleft is a likely source of released water molecules.
    • The Mg-ATP actin conformation, being more closed, sequesters water differently than the Ca-ATP form.