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Updated: Aug 9, 2026

Direct Restart of a Replication Fork Stalled by a Head-On RNA Polymerase
Published on: April 30, 2010
Structure of the RTP-DNA complex and the mechanism of polar replication fork arrest
J A Wilce1, J P Vivian, A F Hastings
1Department of Chemistry/Biochemistry University of Western Australia and the Western Australian Institute for Medical Research, Nedlands, Western Australia 6907 Australia.
Abstract:
The coordinated termination of DNA replication is an important step in the life cycle of bacteria with circular chromosomes, but has only been defined at a molecular level in two systems to date. Here we report the structure of an engineered replication terminator protein (RTP) of Bacillus subtilis in complex with a 21 base pair DNA by X-ray crystallography at 2.5 A resolution. We also use NMR spectroscopic titration techniques. This work reveals a novel DNA interaction involving a dimeric 'winged helix' domain protein that differs from predictions. While the two recognition helices of RTP are in close contact with the B-form DNA major grooves, the 'wings' and N-termini of RTP do not form intimate contacts with the DNA. This structure provides insight into the molecular basis of polar replication fork arrest based on a model of cooperative binding and differential binding affinities of RTP to the two adjacent binding sites in the complete terminator.
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