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Actin-like protein associated with plasma membranes from Euglena gracilis

Petersen-Mahrt, Silja; Sonesson, Anders LU and Widell, Susanne LU (1998) In Protoplasma 202(3-4). p.153-160
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Actin, Anti-actin antibody, Cytoskeleton, Euglena gracilis, Triton X-114, DNAse I
in
Protoplasma
volume
202
issue
3-4
pages
153 - 160
publisher
Springer
external identifiers
  • scopus:0031839279
ISSN
1615-6102
DOI
10.1007/BF01282543
language
English
LU publication?
yes
id
c80c4c40-206a-4a63-a408-de39707c7cf7 (old id 4438048)
alternative location
http://dx.doi.org/10.1007/BF01282543
date added to LUP
2014-05-21 11:47:21
date last changed
2017-01-01 07:35:27
@article{c80c4c40-206a-4a63-a408-de39707c7cf7,
  abstract     = {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.},
  author       = {Petersen-Mahrt, Silja and Sonesson, Anders and Widell, Susanne},
  issn         = {1615-6102},
  keyword      = {Actin,Anti-actin antibody,Cytoskeleton,Euglena gracilis,Triton X-114,DNAse I},
  language     = {eng},
  number       = {3-4},
  pages        = {153--160},
  publisher    = {Springer},
  series       = {Protoplasma},
  title        = {Actin-like protein associated with plasma membranes from Euglena gracilis},
  url          = {http://dx.doi.org/10.1007/BF01282543},
  volume       = {202},
  year         = {1998},
}