Dr. Rahul Jaiswal, Instructor, Virginia Commonwealth University School of Medicine will talk about his work on Cryo-EM studies of a malleable oligomeric SF3 helicase
Talk Abstract: The adeno-associated virus (AAV) non-structural Rep proteins catalyze all the DNA transactions required for virus viability including, DNA replication, transcription regulation, genome packaging, and during a latent phase, site-specific integration. Rep proteins contain two multifunctional domains: An Origin Binding Domain (OBD) and a SF3 helicase domain (HD). Studies have shown that Rep proteins have a dynamic oligomeric behavior where the nature of the DNA substrate molecule modulates its oligomeric state. Thus, Rep68 can form structures ranging from octamers, heptamers and hexamer rings. Assembly on double-stranded DNA substrates leads to formation of a heptameric ring complex that provides insights into the DNA melting mechanism.