Synopsis
DnaA and DnaC are specifically required at the stage of initiation of DNA replication from the E. coli replication origin (oriC) to load the replicative DNA helicase (DnaB) at this chromosomal site. Each of these proteins is multifunctional. DnaA is a protein that binds ATP and also DNA, but in a sequence-specific manner. Additionally, DnaA interacts with other proteins and with acidic phospholipids. Like DnaA, DnaC and DnaB bind ATP. DnaB and DnaC also form a complex with each other. Structure-function studies reveal how the respective protein’s activities are coordinated during the initiation stage of DNA replication.
Introduction
DnaA, DnaB, and DnaC act together to establish the replication fork machinery at oriC. Studies of each protein reveal that they possess specific biochemical activities that can be assigned to distinct structural domains (Fig. 1). ATP binding by each protein is critical for activity, and individual domains involved in nucleotide binding have been...
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I thank the members of my lab for their support while I was writing. This work is supported by Grant GM090063 from the National Institutes of Health and by the Michigan Agricultural Experiment Station.
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Kaguni, J.M. (2014). DnaA, DnaB, and DnaC. In: Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_142-1
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