Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis
The Bacillus subtilis DnaI, DnaB and DnaD proteins load the replicative ring helicase DnaC onto DNA during priming of DNA replication. Here we show that DnaI consists of a C-terminal domain (Cd) with ATPase and DNA-binding activities and an N-terminal domain (Nd) that interacts with the replicative ring helicase. A Zn2+-binding module mediates the interaction with the helicase and C67, C70 and H84 are involved in the coordination of the Zn2+. DnaI binds ATP and exhibits ATPase activity that is...[Show more]
|Collections||ANU Research Publications|
|Source:||Nucleic Acids Research|
|Ioannou_Helicase2006.pdf||2.09 MB||Adobe PDF|
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