Event Title
Mapping the Beta-Sheet Structure of the Yeast Prion Sup35 through Creation of Targeted Mutant Forms
Faculty Sponsor
Kyle MacLea
Location
Jereld R. Nicholson Library
Date
5-17-2013 3:00 PM
End Date
5-17-2013 4:30 PM
Subject Area
Biology
Description
Proteins with an aggregated form rich in beta-sheet structure are known as amyloids, of which a subset are infectious. These infectious proteins are known as prions and cause diseases including bovine spongiform encephalopathy (“Mad Cow” disease). Several prions have been identified in the baker’s yeast, Saccharomyces cerevisiae. One of the most well-studied yeast prions is the protein Sup35. To understand the fine protein structure of Sup35 better, we used PCR-based mutagenesis to introduce a lysine residue (a charged amino acid) at five defined places in the protein sequence of Sup35. We describe our process for creating these mutant versions and the results of DNA sequencing of each mutant version. The next step will be to assess prion formation and stability of clones with the correct sequences. Understanding the behavior of yeast prions has proven helpful in understanding human amyloid diseases and further studies on these yeast prions, including Sup35, will expand our knowledge further.
Recommended Citation
Davis, Emily K.; Knox, James D.; and Palacios, Daniel, "Mapping the Beta-Sheet Structure of the Yeast Prion Sup35 through Creation of Targeted Mutant Forms" (2013). Science and Social Sciences. Event. Submission 17.
https://digitalcommons.linfield.edu/studsymp_sci/2013/all/17
Mapping the Beta-Sheet Structure of the Yeast Prion Sup35 through Creation of Targeted Mutant Forms
Jereld R. Nicholson Library
Proteins with an aggregated form rich in beta-sheet structure are known as amyloids, of which a subset are infectious. These infectious proteins are known as prions and cause diseases including bovine spongiform encephalopathy (“Mad Cow” disease). Several prions have been identified in the baker’s yeast, Saccharomyces cerevisiae. One of the most well-studied yeast prions is the protein Sup35. To understand the fine protein structure of Sup35 better, we used PCR-based mutagenesis to introduce a lysine residue (a charged amino acid) at five defined places in the protein sequence of Sup35. We describe our process for creating these mutant versions and the results of DNA sequencing of each mutant version. The next step will be to assess prion formation and stability of clones with the correct sequences. Understanding the behavior of yeast prions has proven helpful in understanding human amyloid diseases and further studies on these yeast prions, including Sup35, will expand our knowledge further.