The molecular details of the bacterial helicase-primase complex

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DNA replication is one of the most fundamental functions of all living organisms. Understanding the basic mechanisms of action of bacterial DNA replication will be essential not only to extrapolate our findings to the more complex eukaryotic organisms, but also to design new antibacterials in our fight against antibiotic resistance. The helicase-primase complex is a ubiquitous and essential bacterial complex. Our current understanding of the molecular basis of its functions is poorly understood. Recently we have solved the structure of the helicase-interacting domain of the B. stearothermophilus primase protein and we discovered that this domain is structurally homologous to the N-terminal domain of the helicase itself. This was a surprising discovery and one that led us to propose a model to try and explain how the bacterial helicase-primase complex functions. We are now seeking funding to test directly the validity of this model with a series of biochemical experiments. The results of this research will enable us to understand the molecular details of this important complex and will pave the way for the design of new antibacterial drugs that will target this complex and thus bacterial DNA replication.