University of Groningen
Dynamics of the bacterial replisome
Monachino, Enrico
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Publication date: 2018
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Monachino, E. (2018). Dynamics of the bacterial replisome: Biochemical and single-molecule studies of the replicative helicase in Escherichia coli. University of Groningen.
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P
ROPOSITIONSACCOMPANYING THE THESIS
“D
YNAMICS OF THE BACTERIAL REPLISOME”
BY
E
NRICOM
ONACHINO1. Instead of deterministic pathways, multi-protein complexes seem to perform their tasks by choosing from a multitude of pathways, each made possible by the constellation of weak and strong interactions that hold such a complex together (Chapter 1).
2. Single-molecule techniques follow the reaction trajectories of individual molecules and have tremendous power to resolve the fine details of multi-step pathways (Chapter 2).
3. We demonstrate the presence of a novel exchange mechanism that allows Pol III* to remain stably associated with the replisome under conditions of high dilution, yet facilitates rapid exchange at physiological concentrations (Chapter 5).
4. Our observations point to a model in which interaction of the primase with the helicase acts as a switch to control the integrity of the replisome, with implications for the coordination of leading- and lagging-strand synthesis, coupling between polymerase and helicase, and timing of Okazaki-fragment synthesis (Chapter 6).
5. The intrinsic stochasticity that underlies replisome function follows a well-defined design: the replisome evolved to be flexible and, ultimately, capable to react and adapt (Preface to the Thesis).
6. The cryptic CLC-binding pocket in DnaB is a cryptic -binding site (Chapter 7). 7. What is perfection? The E. coli replisome is not a Ferrari, but nonetheless it is a
perfect machine!
8. It is what it is. But we still need to understand it.
9. Do not believe something just because you can explain it (A. Kornberg. Ten Commandments: Lessons from the Enzymology of DNA Replication. J. Bacteriol., 2000 Jul, 182 (13), 3613–3618).
