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ActA is a dimer

P Mourrain1, I Lasa, A Gautreau

  • 1Unité des Interactions Bactéries-Cellules, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France.

Proceedings of the National Academy of Sciences of the United States of America
|September 18, 1997
PubMed
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The ActA surface protein of Listeria monocytogenes forms dimers, a process crucial for actin polymerization and bacterial movement within host cells. This dimerization is mediated by a specific region of the ActA N-terminal domain.

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Listeria monocytogenes utilizes the ActA surface protein to induce actin polymerization, facilitating its intracellular motility.
  • The N-terminal domain of ActA is known to be sufficient for driving actin tail formation.

Purpose of the Study:

  • To investigate the oligomeric state of the ActA protein from Listeria monocytogenes.
  • To determine the role of ActA dimerization in actin polymerization and bacterial motility.

Main Methods:

  • Yeast two-hybrid system to assess ActA homodimerization.
  • Chemical cross-linking to analyze ActA multimerization on bacterial surfaces.
  • Analysis of ActA variants to identify critical regions for dimerization.

Related Experiment Videos

Main Results:

  • The N-terminal domain of ActA can form homodimers.
  • ActA exists as a dimer on the surface of Listeria monocytogenes.
  • Amino acids 97-126 within the ActA N-terminal domain are essential for both dimer formation and actin tail generation.

Conclusions:

  • ActA functions as a dimer to promote actin polymerization, driving Listeria monocytogenes motility.
  • The identified dimerization region is a key determinant of ActA's function in host cell invasion.