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Related Experiment Videos

GTP-yeast actin.

Kuo-Kuang Wen1, Xiaoyi Yao, Peter A Rubenstein

  • 1Department of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242, USA.

The Journal of Biological Chemistry
|August 23, 2002
PubMed
Summary
This summary is machine-generated.

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Yeast actin can bind and hydrolyze GTP, though less tightly than ATP. This study reveals key differences in yeast actin

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Actin proteins are essential cytoskeletal components.
  • While muscle actin primarily uses ATP, other actin superfamily members can use GTP.
  • Yeast actin's conformational flexibility suggests potential GTP utilization.

Purpose of the Study:

  • To investigate the functional capacity of yeast actin with guanosine triphosphate (GTP).
  • To compare GTP binding and hydrolysis in yeast actin versus muscle actin.
  • To elucidate the structural and functional consequences of GTP binding in yeast actin.

Main Methods:

  • Etheno-ATP exchange assays to determine nucleotide binding affinity.
  • Proteolysis and circular dichroism (CD) studies for conformational analysis.

Related Experiment Videos

  • Polymerization assays and electron microscopy to assess filament formation.
  • Site-directed mutagenesis to investigate nucleotide discrimination.

    • Main Results:

    • Yeast actin binds GTP with 1/9 the affinity of ATP, unlike muscle actin (1/1,240).
    • GTP-bound yeast actin shows similar subdomain 2 conformation but reduced thermostability compared to ATP-bound actin.
    • GTP-actin polymerization occurs at a higher critical concentration (1.5 µM) than ATP-actin (0.3 µM), with similar filament structures.
    • Yeast actin hydrolyzes GTP polymerization-dependently, and GTP-F-actin interacts with myosin S1.
    • Mutating Phe(306) to Tyr significantly increased nucleotide discrimination, supporting modeling of the binding site.

    Conclusions:

    • Yeast actin exhibits functional plasticity, utilizing both ATP and GTP.
    • Differences in the nucleotide-binding pocket, particularly residue 306, dictate GTP/ATP discrimination.
    • These findings expand our understanding of actin's versatile nucleotide interactions in different species.