Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy

Publication Type:
Journal Article
Citation:
Biochemical and Biophysical Research Communications, 2005, 335 (2), pp. 361 - 366
Issue Date:
2005-09-23
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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 in1H-15N correlation spectra of a15N-labelled RTP.C110S mutant upon the addition of a 21 base pair symmetrical DNA binding site. Assignment of the1H-15N correlations was achieved using a suite of triple resonance NMR experiments with15N,13C,70%2H enriched protein recorded at 800 MHz and using TROSY pulse sequences. Perturbations to1H-15N spectra revealed that the N-termini, α3-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. © 2005 Elsevier Inc. All rights reserved.
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