“How a largely disordered protein sets the speed of eukaryotic DNA replication”

 

Abstract: When our cells divide an enormous quantity of DNA must first be accurately duplicated. This task is performed by the chromosome replication machinery, collectively termed the replisome. Replisomes possess all the biochemical activities required for fast and efficient DNA replication including DNA helicases, DNA polymerases, ATP-dependent protein remodelers and histone chaperones. To understand how these activities are orchestrated, we reconstitute replisomes from purified yeast and human proteins for analysis in functional DNA replication assays and by cryo-EM. During my talk I will focus on how the rate of replisome progression is controlled through the coordination of DNA helicase and DNA polymerase activities, and how a conserved protein that lacks any tertiary structure plays a critical role in this process.