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Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 1 | Page No.: 76-81
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Research Article

An Exceptionally Short α-actinin-like Protein from the Protozoan Parasite Entamoeba histolytica

Heike Bruhn, Thomas Jacobs, Britta Urban and Matthias Leippe

ABSTRACT

For a primitive phagocytosing cell such as the protozoan Entamoeba histolytica, dynamic fluctuations of the cytoskeleton are crucial for morphological changes involved in cellular movement as well as in phagocytosis. Both activities are implicated in the virulence of the human pathogen. Here, this study molecularly cloned an amoebic α-actinin,one of the components essential for actin bundling. The isolated cDNA codes for a protein of 537 amino acid residues, which displays two calponin homology (CH) domains and three EF-hand motifs. Although obviously belonging to the α-actinin-family, the proein has several features unusual for an α-actinin concerning its domain architecture. Structurally, this protein is the shortest member of the α-actinin family known so far.
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REFERENCES

  1. Guillen, N., 1996. Role of signaling and cytoskeletal rearrangements in the pathogenesis of Entamoeba histolytica. Trends Microbiol., 4: 191-197.
  2. Vazquez, J., E. Franco, G. Reyes and I. Meza, 1995. Characterization of adhesion plates induced by the interaction of Entamoeba histolytica trophozoites with fibronectin. Cell Motility Cytoskeleton, 32: 37-45.
  3. Bailey, G.B., P.S. Shen, M.J. Beanan and N.E. McCoomer, 1992. Actin associated proteins of Entamoeba histolytica. Arch. Med. Res., 23: 129-132.
  4. Vargas, M., P. Sansonetti and N. Guillen, 1996. Identification and cellular localization of the actin-binding protein ABP-120 from Entamoeba histolytica. Mol. Microbiol., 22: 849-857.
  5. Vargas, M., H. Voigt, P. Sansonetti and N. Guillen, 1997. Molecular characterization of myosin IB from the lower eukaryote Entamoeba histolytica, a human parasite. Mol. Biochem. Parasitol., 86: 61-73.
  6. Binder, M., S. Ortner, H. Erben, O. Scheiner, G. Wiedermann, R. Valenta and M. Duchene, 1995. The basic isoform of profilin in pathogenic Entamoeba histolytica. cDNA cloning, heterologous expression and actin-binding properties. Eur. J. Biochem., 233: 976-981.
  7. Ebert, F., N. Guillen, M. Leippe and E. Tannich, 2000. Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins. Mol. Biochem. Parasitol., 111: 459-464.
  8. Matsudaira, P., 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci., 16: 87-92.
  9. Olski, T.M., A.A. Noegel and E. Korenbaum, 2001. Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J. Cell Sci., 114: 525-538.
    Direct Link
  10. Puius, Y.A., N.M. Mahoney and S.C. Almo, 1998. The modular structure of actin-regulatory proteins. Curr. Opin. Cell Biol., 10: 23-34.
  11. Otey, C.A. and O. Carpen, 2004. α-actinin revisited: A fresh look at an old player. Cell. Motility Cytoskeleton, 58: 104-111.
    Direct Link
  12. Lupas, A., M. van Dyke and J. Stock, 1991. Predicting coiled coils from protein sequences. Science, 252: 1162-1164.
  13. Berger, B., D.B. Wilson, E. Wolf, T. Tonchev, M. Milla and P.S. Kim, 1995. Predicting coiled coils by use of pairwise residue correlations. Proc. Natl. Acad. Sci. USA., 92: 8259-8263.
  14. Wolf, E., P.S. Kim and B. Berger, 1997. MultiCoil: A program for predicting two- and three-stranded coiled coils. Protein Sci., 6: 1179-1189.
    Direct Link
  15. Guex, N. and M.C. Peitsch, 1997. SWISS-MODEL and the Swiss-PDB viewer: An environment for comparative protein modeling. Electrophoresis, 18: 2714-2723.
    CrossRefPubMedDirect Link
  16. Nickel, R., T. Jacobs, B. Urban, H. Scholze, H. Bruhn and M. Leippe, 2000. Two novel calcium-binding proteins from cytoplasmic granules of the protozoan parasite Entamoeba histolytica. FEBS Lett., 486: 112-116.
  17. Gimona, M., K. Djinovic-Carugo, W.J. Kranewitter and S.J. Winder, 2002. Functional plasticity of CH domains. FEBS Lett., 513: 98-106.
  18. Banuelos, S., M. Saraste and K.D. Carugo, 1998. Structural comparisons of calponin homology domains: Implications for actin binding. Structure, 6: 1419-1431.
  19. Bricheux, G., G. Coffe, N. Pradel and G. Brugerolle, 1998. Evidence for an uncommon α-actinin protein in Trichomonas vaginalis. Mol. Biochem. Parasitol., 95: 241-249.
  20. Wang, C.L., J.M. Chalovich, P. Graceffa, R.C. Lu, K. Mabuchi and W.F. Stafford, 1991. A long helix from the central region of smooth muscle caldesmon. J. Biol. Chem., 266: 13958-13963.
  21. Wang, E. and C.L. Wang, 1996. (i, i + 4) Ion pairs stabilize helical peptides derived from smooth muscle caldesmon. Arch. Biochem. Biophys., 329: 156-162.
    Direct Link
  22. Djinovic-Carugo, K., P. Young, M. Gautel and M. Saraste, 1999. Structure of the α-actinin rod: Molecular basis for cross-linking of actin filaments. Cell, 98: 537-546.
  23. Matsudaira, P., 1994. Actin crosslinking proteins at the leading edge. Semin. Cell Biol., 5: 165-174.
  24. Franco, E., R. Manning-Cela and I. Meza, 2002. Signal transduction in Entamoeba histolytica induced by interaction with fibronectin: Presence and activation of phosphokinase A and its possible relation to invasiveness. Arch. Med. Res., 33: 389-397.
    Direct Link
  25. Meza, I., 2000. Extracellular matrix-induced signaling in Entamoeba histolytica: Its role in invasiveness. Parasitol. Today, 16: 23-28.
  26. Djinovic-Carugo, K., M. Gautel, J. Ylanne and P. Young, 2002. The spectrin repeat: A structural platform for cytoskeletal protein assemblies. FEBS Lett., 513: 119-123.
  27. Ylanne, J., K. Scheffzek, P. Young and M. Saraste, 2001. Crystal structure of the α-actinin rod reveals an extensive torsional twist. Structure, 9: 597-604.
    Direct Link
  28. Thompson, J.D., D.G. Higgins and T.J. Gibson, 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22: 4673-4680.
    CrossRefPubMedDirect Link

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