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The ubiquitous sliding clamp facilitates processivity of the replicative polymerase and acts as a platform to recruit proteins involved in replication, recombination and repair. While the dynamics of the  E. coli β  2 -sliding clamp have been characterized  in vitro , its  in vivo  stoichiometry and dynamics remain unclear. To probe both  β  2 -clamp dynamics and stoichiometry in live  E. coli  cells, we use custom-built microfluidics in combination with single-molecule fluorescence microscopy and photoactivated fluorescence microscopy. We quantify the recruitment, binding and turnover of  β  2 -sliding clamps on DNA during replication. These quantitative  in vivo  results demonstrate that numerous  β  2 -clamps in  E. coli  remain on the DNA behind the replication fork for a protracted period of time, allowing them to form a docking platform for other enzymes involved in DNA metabolism.

Slow unloading leads to DNA-bound β2-sliding clamp accumulation in live Escherichia coli cells