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Published online 1 June 2004

Nucleic Acids Research, 2004, Vol. 32, No. 10 2977-2986
© 2004 Oxford University Press

DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings

Jenny Thirlway, Ian J. Turner1, Christopher T. Gibson1, Laurence Gardiner, Kevin Brady, Stephanie Allen1, Clive J. Roberts1 and Panos Soultanas*

Centre for Biomolecular Sciences (CBS) and 1 Laboratory of Biophysics and Surface Analysis (LBSA), School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, UK

*To whom correspondence should be addressed. Tel: +44 115 9513525; Fax: +44 115 9513564; Email: panos.soultanas{at}nottingham.ac.uk

Received April 8, 2004; Revised and Accepted May 11, 2004

Loading of the replicative ring helicase onto the origin of replication (oriC) is the final outcome of a well coordinated series of events that collectively constitute a primosomal cascade. Once the ring helicase is loaded, it recruits the primase and signals the switch to the polymerization mode. The transient nature of the helicase–primase (DnaB–DnaG) interaction in the Escherichia coli system has hindered our efforts to elucidate its structure and function. Taking advantage of the stable DnaB–DnaG complex in Bacillus stearothermophilus, we have reviewed conflicting mutagenic data from other bacterial systems and shown that DnaG interacts with the flexible linker that connects the N- and C-terminal domains of DnaB. Furthermore, atomic force microscopy (AFM) imaging experiments show that binding of the primase to the helicase induces predominantly a 3-fold symmetric morphology to the hexameric ring. Overall, three DnaG molecules appear to interact with the hexameric ring helicase but a small number of complexes with two and even one DnaG molecule bound to DnaB were also detected. The structural/functional significance of these data is discussed and a speculative structural model for this complex is suggested.


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