On the specificity of interaction between the Saccharomyces cerevisiae clamp loader replication factor C and primed DNA templates during DNA replication.

摘要: Abstract Replication factor C (RFC) catalyzes assembly of circular proliferating cell nuclear antigen clamps around primed DNA, enabling processive synthesis by DNA polymerase during replication and repair. In order to perform this function efficiently, RFC must rapidly recognize as the substrate for clamp assembly, particularly lagging strand synthesis. Earlier reports well quantitative binding experiments from study indicate, however, that interacts with primer-template single- double-stranded (ssDNA dsDNA, respectively) similar high affinity (apparent K d ≈ 10 nm). How then can distinguish sites excess ssDNA dsDNA at fork? Further analysis reveals despite its various structures, selects even in presence a 50-fold dsDNA. The interaction between or is far less stable than (k off > 0.2 s−1 versus 0.025 s−1, respectively). We propose ability bind release coupled selective, allows scan efficiently where it pause initiate assembly.