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Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA

Lookup NU author(s): Graham Scholefield, Professor Jeff ErringtonORCiD, Professor Heath MurrayORCiD

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Abstract

Control of DNA replication initiation is essential for normal cell growth. A unifying characteristic of DNA replication initiator proteins across the kingdoms of life is their distinctive AAA + nucleotide-binding domains. The bacterial initiator DnaA assembles into a right-handed helical oligomer built upon interactions between neighbouring AAA + domains, that in vitro stretches DNA to promote replication origin opening. The Bacillus subtilis protein Soj/ParA has previously been shown to regulate DnaA-dependent DNA replication initiation; however, the mechanism underlying this control was unknown. Here, we report that Soj directly interacts with the AAA + domain of DnaA and specifically regulates DnaA helix assembly. We also provide critical biochemical evidence indicating that DnaA assembles into a helical oligomer in vivo and that the frequency of replication initiation correlates with the extent of DnaA oligomer formation. This work defines a significant new regulatory mechanism for the control of DNA replication initiation in bacteria. The EMBO Journal (2012) 31, 1542-1555. doi:10.1038/emboj.2012.6; Published online 27 January 2012

Publication metadata

Author(s): Scholefield G, Errington J, Murray H

Publication type: Article

Publication status: Published

Journal: EMBO Journal

Year: 2012

Volume: 31

Issue: 6

Pages: 1542-1555

Print publication date: 27/01/2012

ISSN (print): 0261-4189

ISSN (electronic): 1460-2075

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1038/emboj.2012.6

DOI: 10.1038/emboj.2012.6

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