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Updated: Aug 16, 2026

Imaging Mismatch Repair and Cellular Responses to DNA Damage in Bacillus subtilis
Published on: February 8, 2010
Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy
Adam F Hastings1, Gottfried Otting, Rutger H A Folmer
1School of Molecular and Microbial Biosciences, University of Sydney, Sydney, NSW 2006, Australia.
Abstract:
Termination of DNA replication in Bacillus subtilis involves the polar arrest of replication forks by a specific complex formed between the dimeric 29 kDa replication terminator protein (RTP) and DNA terminator sites. We have used NMR spectroscopy to probe the changes in 1H-15N correlation spectra of a 15N-labelled RTP.C110S mutant upon the addition of a 21 base pair symmetrical DNA binding site. Assignment of the 1H-15N correlations was achieved using a suite of triple resonance NMR experiments with 15N,13C,70% 2H enriched protein recorded at 800 MHz and using TROSY pulse sequences. Perturbations to 1H-15N spectra revealed that the N-termini, alpha3-helices and several loops are affected by the binding interaction. An analysis of this data in light of the crystallographically determined apo- and DNA-bound forms of RTP.C110S revealed that the NMR spectral perturbations correlate more closely to protein structural changes upon complex formation rather than to interactions at the protein-DNA interface.
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