BYU

Abstract by Theresa Smith

Personal Infomation


Presenter's Name

Theresa Smith

Co-Presenters

None

Degree Level

Doctorate

Co-Authors

None

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

Barry Willardson

Title

The role of CCT in folding the crucial visual cycle protein, RPE65

Abstract

RPE65 is a critical isomerase involved in the regeneration of 11-cis-retinal, a photosensitive molecule required for vision. Mutations in RPE65 are linked to mild to severe retinal degenerative diseases including Leber congenital amaurosis (LCA), which often leads to blindness in early childhood. However, little is known about how RPE65 gets folded. We are investigating a novel interaction between RPE65 and the cytosolic chaperonin, CCT. SgRNA knockdown of CCT results in reduced RPE65 expression indicating that it contributes to RPE65 folding. A high-resolution cryo-EM structure of this complex will help to fully elucidate the role of CCT and may contribute to an improved understanding of RPE65 pathogenesis.