Zawilak A, Durrant MC, Jakimowicz P, Backert S, Zakrzewska-Czerwińska J (2003)
Publication Type: Journal article
Publication year: 2003
Book Volume: 334
Pages Range: 933-947
Journal Issue: 5
DOI: 10.1016/j.jmb.2003.10.018
The key protein in the initiation of Helicobacter pylori chromosome replication, DnaA, has been characterized. The amount of the DnaA protein was estimated to be approximately 3000 molecules per single cell; a large part of the protein was found in the inner membrane. The H.pylori DnaA protein has been analysed using in vitro (gel retardation assay and surface plasmon resonance (SPR)) as well as in silico (comparative computer modeling) studies. DnaA binds a single DnaA box as a monomer, while binding to the fragment containing several DnaA box motifs, the oriC region, leads to the formation of high molecular mass nucleoprotein complexes. In comparison with the Escherichia coli DnaA, the H.pylori DnaA protein exhibits lower DNA-binding specificity; however, it prefers oriC over non-box DNA fragments. As determined by gel retardation techniques, the H.pylori DnaA binds with a moderate level of affinity to its origin of replication (4nM). Comparative computer modelling showed that there are nine residues within the binding domain which are possible determinants of the reduced H.pylori DnaA specificity. Of these, the most interesting is probably the triad PTL; all three residues show significant divergence from the consensus, and Thr398 is the most divergent residue of all. © 2003 Elsevier Ltd. All rights reserved.
APA:
Zawilak, A., Durrant, M.C., Jakimowicz, P., Backert, S., & Zakrzewska-Czerwińska, J. (2003). DNA Binding Specificity of the Replication Initiator Protein, DnaA from Helicobacter pylori. Journal of Molecular Biology, 334(5), 933-947. https://dx.doi.org/10.1016/j.jmb.2003.10.018
MLA:
Zawilak, Anna, et al. "DNA Binding Specificity of the Replication Initiator Protein, DnaA from Helicobacter pylori." Journal of Molecular Biology 334.5 (2003): 933-947.
BibTeX: Download