The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Actin-like protein associated with plasma membranes from Euglena gracilis

Author

Summary, in English

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.

Publishing year

1998

Language

English

Pages

153-160

Publication/Series

Protoplasma

Volume

202

Issue

3-4

Document type

Journal article

Publisher

Springer

Topic

  • Biological Sciences

Keywords

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

Status

Published

ISBN/ISSN/Other

  • ISSN: 1615-6102