Presentation Title

Increased Number of CAG Repeats in the Human HTT Gene Causes More Protein Aggregation in Saccharomyces cerevisiae

Faculty Mentor

Nieves Lorenzo, Anna Alcaine-Colet

Start Date

17-11-2018 8:30 AM

End Date

17-11-2018 10:30 AM

Location

CREVELING 48

Session

POSTER 1

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

Increased Number of CAG Repeats in the Human HTT Gene Causes More Protein Aggregation in Saccharomyces cerevisiae

Author: Leah Soldner-García

Mentor(s): Nieves Lorenzo and Anna Alcaine, Center for Genomic Regulation, Barcelona

Huntington’s disease, caused by an increased number of CAG repeats in the Huntingtin gene, is a dominantly transferred incurable neurogenerative disorder, meaning that the children of HD patients have a 50% chance of getting the disease. When the HTT gene is translated into the HTT protein, the abnormal number of repeats (usually 36 or more) results in an elongated polyglutamine (polyQ) chain, creating aggregates of the protein inside the cell. Research suggests that it is still unclear whether the cause of Huntington’s is the lengthened form of the HTT gene or the protein aggregation. To see if Huntington’s disease toxicity occurs at the protein level, we wanted to find out whether increasing number of repeats cause more protein aggregation and an increase in intracellular toxicity. Using Saccharomyces cerevisiae,we transformed the yeast to have differing numbers of CAG repeats—25Q, 46Q, and 103Q. Growing them over a few days, we did growth assays to determine the severity of different protein aggregations (WT, 25Q, 46Q, 103Q). Through doing western blots and microscopy, we saw that the increasing number of repeats led to more protein aggregation. However, we could not conclude whether protein aggregation still leads to cell toxicity, due to the short time span of the research, therefore more research to answer this question, is needed.

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Nov 17th, 8:30 AM Nov 17th, 10:30 AM

Increased Number of CAG Repeats in the Human HTT Gene Causes More Protein Aggregation in Saccharomyces cerevisiae

CREVELING 48

Increased Number of CAG Repeats in the Human HTT Gene Causes More Protein Aggregation in Saccharomyces cerevisiae

Author: Leah Soldner-García

Mentor(s): Nieves Lorenzo and Anna Alcaine, Center for Genomic Regulation, Barcelona

Huntington’s disease, caused by an increased number of CAG repeats in the Huntingtin gene, is a dominantly transferred incurable neurogenerative disorder, meaning that the children of HD patients have a 50% chance of getting the disease. When the HTT gene is translated into the HTT protein, the abnormal number of repeats (usually 36 or more) results in an elongated polyglutamine (polyQ) chain, creating aggregates of the protein inside the cell. Research suggests that it is still unclear whether the cause of Huntington’s is the lengthened form of the HTT gene or the protein aggregation. To see if Huntington’s disease toxicity occurs at the protein level, we wanted to find out whether increasing number of repeats cause more protein aggregation and an increase in intracellular toxicity. Using Saccharomyces cerevisiae,we transformed the yeast to have differing numbers of CAG repeats—25Q, 46Q, and 103Q. Growing them over a few days, we did growth assays to determine the severity of different protein aggregations (WT, 25Q, 46Q, 103Q). Through doing western blots and microscopy, we saw that the increasing number of repeats led to more protein aggregation. However, we could not conclude whether protein aggregation still leads to cell toxicity, due to the short time span of the research, therefore more research to answer this question, is needed.