Photos from the 2003 East Tennessee Collegiate Division Meeting of the Tennessee Academy of Science held at Pellissippi State Technical Community College
4/11/2003
William Thompson, Lee University
Second Place Outstanding Undergraduate Presentation
ABSTRACT
Exploring Novel Protein Interactions Involving ARC in a Yeast Two-Hybrid System
ARC (Apoptosis Repressor protein with CARD domain) has been shown to inhibit both apoptosis and necrosis through interactions with initiator caspases and by preserving mitochondrial membrane potential and blocking cytochrome C release. ARC contains a caspase recruitment domain (CARD) which interacts with proximal caspases. In this study we have identified several protein-protein interactions involving ARC which are mediated through the CARD domain. By using a Yeast Two-Hybrid System, we show that the CARD domain of ARC has a strong dimeric interaction. Furthermore, the L31F mutant of ARC has a decreased level of dimerization compared to the ARC-CARD/ARC-CARD interaction. In contrast, the G70R mutant of ARC gave the strongest dimeric interaction of all the ARC interactions tested. Here we show that, compared to
wild-type ARC-CARD/ARC-CARD, the L31F mutant has a five fold decrease in the level of dimerization while the G70R mutant shows a seven fold increase in the dimerization interaction.
