Abstract
Rep helicase interacts with PriC and single-stranded DNA binding proteins (SSB) to remodel the DNA at a stalled replication fork. Within a crowded and dynamic cellular interior, Rep, PriC, and SSB compete for access to DNA with proteins from other replication restart and repair pathways. Imprecise orchestration of protein-protein interactions can lead to genomic instability, but how precise coordination is accomplished is not well understood. Using a dual-optical trap we assessed the regulatory role of protein-protein interactions and fork geometry on Rep helicase.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
