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Related Experiment Videos

Primary sequence independence for prion formation.

Eric D Ross1, Herman K Edskes, Michael J Terry

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 27, 2005
PubMed
Summary
This summary is machine-generated.

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Protein prion formation in yeast, like [URE3] and [PSI+], depends on amino acid composition, not specific sequences. Shuffled protein domains can still form infectious amyloid fibrils, suggesting sequence flexibility in prion generation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Proteins can form self-propagating beta-sheet-rich amyloid fibrils.
  • The [URE3] and [PSI+] prions in Saccharomyces cerevisiae are amyloid forms of Ure2p and Sup35p proteins.
  • Ure2p prion formation is influenced by its amino acid sequence composition.

Purpose of the Study:

  • To investigate the role of sequence composition versus specific sequences in prion formation.
  • To determine the influence of fragment length on prion induction.
  • To explore the sequence independence of prion formation in yeast.

Main Methods:

  • Induction of prions using full-length and scrambled Ure2p variants.
  • Analysis of amino acid sequences in inducing fragments.

Related Experiment Videos

  • Randomization of the Sup35p prion domain sequence.

    • Main Results:

    • Prion induction by Ure2p and scrambled Ure2-21p fragments depends on fragment length.
    • No single conserved sequence was found in all inducing Ure2-21p fragments, indicating sequence independence.
    • Randomized Sup35p prion domain sequences retained prion-forming ability, generating multiple prion variants.

    Conclusions:

    • [PSI+] prion formation is primarily driven by the amino acid composition of the Sup35p prion domain.
    • Specific amino acid sequences and oligopeptide repeats are not essential for prion formation or maintenance.