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To mitigate errors induced by the cell's heterogeneous noisy environment, itsmain information channels and production networks utilize the kineticproofreading (KPR) mechanism. Here, we examine two extensively-studied KPRcircuits, DNA replication by the T7 DNA polymerase and translation by the E.coli ribosome. Using experimental data, we analyze the performance of these twovital systems in light of the fundamental bounds set by the recently-discoveredthermodynamic uncertainty relation (TUR), which places an inherent trade-offbetween the precision of a desirable output and the amount of energydissipation required. We show that the DNA polymerase operates close to the TURlower bound, while the ribosome operates $\sim5$ times farther from this bound.This difference originates from the enhanced binding discrimination of thepolymerase which allows it to operate effectively as a reduced reaction cycleprioritizing correct product formation. We show that approaching this limitalso decouples the thermodynamic uncertainty factor from speed and error,thereby relaxing the accuracy-speed trade-off of the system. Altogether, ourresults show that operating near this reduced cycle limit not only minimizesthermodynamic uncertainty, but also results in global performance enhancementof KPR circuits.

Kinetic Proofreading and the Limits of Thermodynamic Uncertainty