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You are here: Home Administration Chemistry & Biochemistry Department Events 2019 February Biochemistry Seminar: Tricia Serio, "Prion Biology:At the Intersection of Protein Folding and its Cellular Environment"

Biochemistry Seminar: Tricia Serio, "Prion Biology:At the Intersection of Protein Folding and its Cellular Environment"

Tricia Serio, Professor, Biochemistry & Molecular Biology, Dean, College of Natural Sciences, University of Massachusetts Amherst, MA, "Prion Biology: At the Intersection of Protein Folding and its Cellular Environment"
When Feb 27, 2019
from 12:00 PM to 01:00 PM
Where CUNY ASRC Main Auditorium
Contact Name
Contact Phone 212-650-8803
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ABSTRACT

The prion hypothesis provides an explanation for a collection of previously inexplicable biological phenomena ranging from the infectivity of neurodegenerative diseases, such as mad cow disease, Creutzfeldt-Jakob disease, and scrapie, in mammals to the non-Mendelian inheritance of unique traits in fungi. According to this idea, prion-associated phenotypes are determined epigenetically by alternative conformations of normal, host-encoded proteins and persist because the alternative conformers are stabilized by their assembly into amyloid, which can template the continued refolding of other conformers of the prion into a like state. In vivo, the efficiency of conformational self-replication is modulated by cellular processes that impact aggregate dynamics.

 

In contrast to the well-studied process of prion persistence, our mechanistic understanding of prion appearance lags far behind. To gain this insight, our studies have focused on the Sup35/[PSI+] prion of S. cerevisiae. The spontaneous appearance of [PSI+] is enhanced by Sup35 overexpression in yeast strains propagating the [RNQ+] prion, suggesting that [PSI+] appearance is limited by forces that can be overcome by Rnq1 aggregates.  While Rnq1 aggregates are thought to template the formation of a stable amyloid nucleus, we find their primary role is to promote amyloid nucleus persistence by rebalancing the interplay between protein aggregation and clearance.

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