Actin-like protein associated with plasma membranes from Euglena gracilis

Silja Petersen-Mahrt, Anders Sonesson, Susanne Widell

Research output: Contribution to journalArticlepeer-review


Microtubules are characteristic components of the membrane skeleton of Euglena gracilis, but whether microfilaments are present has been controversial. We here present evidence that an actin-like protein may indeed be associated with the plasma membrane (PM) of E. gracilis. Firstly, a 47 kDa, PM-associated, polypeptide was recognized by an anti-amoeba actin antibody. Secondly, this 47 kDa protein seemed to be peripherally attached to PM in much the same way as β-tubulin, since both could be released from PM by treatment with 150 mM NaOH but not with ethylene glycol, NaCl, or formamide. Thirdly, the 47 kDa polypeptide and β-tubulin were found mainly in the Triton X-1 14-insoluble fraction, indicating that they were part of a protein complex resistant to detergents, such as the cytoskeleton. Finally, DNase I activity was inhibited by a fraction enriched in the 47 kDa polypeptide, a property typical of actin.
Original languageEnglish
Pages (from-to)153-160
Number of pages8
Issue number3-4
Publication statusPublished - 1998

Bibliographical note

Department affilation moved from v1000887 (CED - Centre for Educational Development) to v1000942 (Division for Higher Education Development) on 2016-03-31 08:48:47.

Subject classification (UKÄ)

  • Biological Sciences

Free keywords

  • Actin
  • Anti-actin antibody
  • Cytoskeleton
  • Euglena gracilis
  • Triton X-114
  • DNAse I


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