Cloning and characterization of actin depolymerizing factor from Toxoplasma gondii

M. Leah Allen, Janice M. Dobrowolski, Hayyah Muller, L. David Sibley, Tag E. Mansour

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65 Scopus citations


We determined the predicted amino acid sequence of actin depolymerizing factor (ADF) from Toxoplasma gondii by sequencing the full-length cDNA. T. gondii ADF consists of 118 amino acids (calculated molecular weight 13 400) and shares a high degree of sequence similarity to other low molecular weight actin monomer sequestering proteins, especially Acanthamoeba actophorin, plant ADFs and yeast and vertebrate cofilin. ADF from T. gondii is smaller and does not contain a nuclear localization sequence like the related vertebrate proteins. Southern blot analysis indicates that T. gondii ADF is a single-copy gene. Homogeneous recombinant T. gondii ADF purified from E. coli is active in binding actin monomers and depolymerizing F-actin. Localization of ADF by immunofluorescence and immunoelectron microscopy indicates ADF is scattered throughout the cytoplasm and prominently localized beneath the plasma membrane in T. gondii.

Original languageEnglish
Pages (from-to)43-52
Number of pages10
JournalMolecular and Biochemical Parasitology
Issue number1-2
StatePublished - Sep 1997


  • Actin depolymerizing factor
  • Cytoskeleton
  • Toxoplasma gondii


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