Nucleic Acids Research Advance Access originally published online on September 26, 2006
Nucleic Acids Research 2006 34(18):5247-5258; doi:10.1093/nar/gkl690
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Nucleic Acids Research, 2006, Vol. 34, No. 18 5247-5258
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis
Centre for Biomolecular Sciences, School of Chemistry, University of Nottingham, University Park Nottingham NG7 2RD, UK 1 Research School of Chemistry, Australian National University Canberra ACT 0200, Australia
*To whom correspondence should be addressed. Tel: +44 115 9513525; Fax: +44 115 8468002; Email: panos.soultanas{at}nottingham.ac.uk
Received June 13, 2006. Revised September 4, 2006. Accepted September 7, 2006.
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 not stimulated by ssDNA, because the DNA-binding site on Cd is masked by Nd. The ATPase activity resides on the Cd domain and when detached from the Nd domain, it becomes sensitive to stimulation by ssDNA because its cryptic DNA-binding site is exposed. Therefore, Nd acts as a molecular ‘switch’ regulating access to the ssDNA binding site on Cd, in response to binding of the helicase. DnaI is sufficient to load the replicative helicase from a complex with six DnaI molecules, so there is no requirement for a dual helicase loader system.
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