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Toxicity of expanded polyglutamine-domain proteins in Escherichia coli.

Publication ,  Journal Article
Onodera, O; Roses, AD; Tsuji, S; Vance, JM; Strittmatter, WJ; Burke, JR
Published in: FEBS Lett
December 9, 1996

Five neurodegenerative diseases are caused by proteins with expanded polyglutamine domains. Toxicity of these proteins has been previously identified only in mammals, and no simple model systems are available. In this paper, we demonstrate in E. coli that long polyglutamine domains (59-81 residues) as GST-fusion proteins inhibit growth while smaller glutamine (10-35 residues) or polyalanine (61 residues) domains have no effect. Analogously in humans, polyglutamine repeats less than 35-40 glutamines produce a normal phenotype, while expansion greater than 40 glutamines is always associated with disease. Expression of polyglutamine proteins in E. coli may help identify the molecular mechanism of pathogenesis of CAG trinucleotide repeat diseases and be a useful screen to identify potential therapeutic compound.

Duke Scholars

Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

December 9, 1996

Volume

399

Issue

1-2

Start / End Page

135 / 139

Location

England

Related Subject Headings

  • Recombinant Fusion Proteins
  • Proteins
  • Peptides
  • Molecular Sequence Data
  • Humans
  • Glutathione Transferase
  • Escherichia coli
  • Cloning, Molecular
  • Biochemistry & Molecular Biology
  • Amino Acid Sequence
 

Citation

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Onodera, O., Roses, A. D., Tsuji, S., Vance, J. M., Strittmatter, W. J., & Burke, J. R. (1996). Toxicity of expanded polyglutamine-domain proteins in Escherichia coli. FEBS Lett, 399(1–2), 135–139. https://doi.org/10.1016/s0014-5793(96)01301-4
Onodera, O., A. D. Roses, S. Tsuji, J. M. Vance, W. J. Strittmatter, and J. R. Burke. “Toxicity of expanded polyglutamine-domain proteins in Escherichia coli.FEBS Lett 399, no. 1–2 (December 9, 1996): 135–39. https://doi.org/10.1016/s0014-5793(96)01301-4.
Onodera O, Roses AD, Tsuji S, Vance JM, Strittmatter WJ, Burke JR. Toxicity of expanded polyglutamine-domain proteins in Escherichia coli. FEBS Lett. 1996 Dec 9;399(1–2):135–9.
Onodera, O., et al. “Toxicity of expanded polyglutamine-domain proteins in Escherichia coli.FEBS Lett, vol. 399, no. 1–2, Dec. 1996, pp. 135–39. Pubmed, doi:10.1016/s0014-5793(96)01301-4.
Onodera O, Roses AD, Tsuji S, Vance JM, Strittmatter WJ, Burke JR. Toxicity of expanded polyglutamine-domain proteins in Escherichia coli. FEBS Lett. 1996 Dec 9;399(1–2):135–139.
Journal cover image

Published In

FEBS Lett

DOI

ISSN

0014-5793

Publication Date

December 9, 1996

Volume

399

Issue

1-2

Start / End Page

135 / 139

Location

England

Related Subject Headings

  • Recombinant Fusion Proteins
  • Proteins
  • Peptides
  • Molecular Sequence Data
  • Humans
  • Glutathione Transferase
  • Escherichia coli
  • Cloning, Molecular
  • Biochemistry & Molecular Biology
  • Amino Acid Sequence