NMR assignment of the conserved bacterial DNA replication protein DnaA domain IV

Chromosomal replication is a ubiquitous and essential cellular process. In bacteria, the master replication initiator DnaA plays a key role in promoting an open complex at the origin ( oriC ) and recruiting helicase in a tightly regulated process. The C-terminal domain IV specifically recognises consensus sequences of double-stranded DNA in oriC , termed DnaA-boxes, thereby facilitating the initial engagement of DnaA to oriC . Here, we report the 13 Cβ and backbone 1 H, 15 N, and 13 C chemical shift assignments of soluble DnaA domain IV from Bacillus subtilis at pH 7.6 and 298 K.