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All Outputs (33)

Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus (2014)
Journal Article
Green, M., Gilhooly, N. S., Abedeen, S., Scott, D. J., Dillingham, M. S., & Soultanas, P. (2014). Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus. Biosensors and Bioelectronics, 61, 579-586. https://doi.org/10.1016/j.bios.2014.06.011

Single-stranded DNA-binding protein (SSB) is a well characterized ubiquitous and essential bacterial protein involved in almost all aspects of DNA metabolism. Using the Bacillus subtilis SSB we have generated a reagentless SSB biosensor that can be u... Read More about Engineering a reagentless biosensor for single-stranded DNA to measure real-time helicase activity in Bacillus.

Pro-inflammatory cytokines can act as intracellular modulators of commensal bacterial virulence (2013)
Journal Article
Mahdavi, J., Royer, P., Sjolinder, H. S., Azimi, S., Self, T., Stoof, J., …Ala'Aldeen, D. A. (2013). Pro-inflammatory cytokines can act as intracellular modulators of commensal bacterial virulence. Open Biology, 3, Article e130048. https://doi.org/10.1098/rsob.130048

Interactions between commensal pathogens and hosts are critical for disease development but the underlying mechanisms for switching between the commensal and virulent states are unknown. We show that the human pathogen Neisseria meningitidis, the lea... Read More about Pro-inflammatory cytokines can act as intracellular modulators of commensal bacterial virulence.

Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis (2013)
Journal Article
Rannou, O., Le Chatelier, E., Larson, M. A., Nouri, H., Dalmais, B., Laughton, C., …Soultanas, P. (2013). Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis. Nucleic Acids Research, 41(10), https://doi.org/10.1093/nar/gkt207

Bacillus subtilis has two replicative DNA polymerases. PolC is a processive high-fidelity replicative polymerase, while the error-prone DnaEBs extends RNA primers before hand-off to PolC at the lagging strand. We show that DnaEBs interacts with t... Read More about Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.

Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase. (2013)
Journal Article
Afonso, J. P., Chintakayala, K., Suwannachart, C., Sedelnikova, S., Giles, K., Hoyes, J. B., …Oldham, N. J. (2013). Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase. Nucleic Acids Research, 41(9), https://doi.org/10.1093/nar/gkt173

The clamp-loader complex plays a crucial role in DNA replication by loading the β-clamp onto primed DNA to be used by the replicative polymerase. Relatively little is known about the stoichiometry, structure and assembly pathway of this complex, an... Read More about Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase..

Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites (2011)
Journal Article
Collier, C., Machon, C., Briggs, G. S., Smits, W. K., & Soultanas, P. (2011). Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites. Nucleic Acids Research, 40(2), https://doi.org/10.1093/nar/gkr785

Bacterial nucleoid associated proteins play a variety of roles in genome maintenance and dynamics. Their involvement in genome packaging, DNA replication and transcription are well documented but it is still unclear whether they play any specific rol... Read More about Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites.

DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis (2010)
Journal Article
Grainger, W. H., Machón, C., Scott, D. J., & Soultanas, P. (2010). DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis. Nucleic Acids Research, 38(9), https://doi.org/10.1093/nar/gkp1236

Initiation of bacterial DNA replication at oriC is mediated by primosomal proteins that act cooperatively to melt an AT-rich region where the replicative helicase is loaded prior to the assembly of the replication fork. In Bacillus subtilis, the dnaD... Read More about DnaB proteolysis in vivo regulates oligomerization and its localization at oriC in Bacillus subtilis.

RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD (2010)
Journal Article
Mach?n, C., Thomson, N., Lynch, G., Scott, D. J., Thomas, C., & Soultanas, P. (2010). RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD. Nucleic Acids Research, 38(6), https://doi.org/10.1093/nar/gkp1153

Plasmid encoded replication initiation (Rep) proteins recruit host helicases to plasmid replication origins. Previously, we showed that RepD recruits directionally the PcrA helicase to the pC221 oriD, remains associated with it, and increases its pro... Read More about RepD-mediated recruitment of PcrA helicase at the Staphylococcus aureus pC221 plasmid replication origin, oriD.

Structure of the N-terminal oligomerization domain of DnaD reveals a unique tetramerization motif and provides insights into scaffold formation (2008)
Journal Article
Schneider, S., Zhang, W., Soultanas, P., & Paoli, M. (2008). Structure of the N-terminal oligomerization domain of DnaD reveals a unique tetramerization motif and provides insights into scaffold formation. Journal of Molecular Biology, 376(5),

DnaD is a primosomal protein that remodels supercoiled plasmids. It binds to supercoiled forms and converts them to open forms without nicking. During this remodeling process, all the writhe is converted to twist and the plasmids are held around the... Read More about Structure of the N-terminal oligomerization domain of DnaD reveals a unique tetramerization motif and provides insights into scaffold formation.

The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA (2006)
Journal Article
Zhang, W., Allen, S., Roberts, C. J., & Soultanas, P. (2006). The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA. Journal of Bacteriology, 188(15), https://doi.org/10.1128/JB.00339-06

The essential Bacillus subtilis DnaD and DnaB proteins have been implicated in the initiation of DNA replication. Recently, DNA remodeling activities associated with both proteins were discovered that could provide a link between global or local nucl... Read More about The Bacillus subtilis primosomal protein DnaD untwists supercoiled DNA.

Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis (2006)
Journal Article
Ioannou, C., Schaeffer, P. M., Dixon, N. E., & Soultanas, P. (2006). Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis. Nucleic Acids Research, 34(18), https://doi.org/10.1093/nar/gkl690

The Bacillus subtilis DnaI, DnaB and DnaD proteins load the replicative ring helicase DnaC onto DNA during priming of DNA replication. Here we show that DnaI consists of a C-terminal domain (Cd) with ATPase and DNA-binding activities and an N-termina... Read More about Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis.

The bacterial helicase-primase interaction: a common structural/functional module (2005)
Journal Article
Soultanas, P. (2005). The bacterial helicase-primase interaction: a common structural/functional module. Structure, 13(6), https://doi.org/10.1016/j.str.2005.04.006

The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two ne... Read More about The bacterial helicase-primase interaction: a common structural/functional module.

Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid (2005)
Journal Article
Gardiner, L., Coyle, B. J., Chan, W. C., & Soultanas, P. (2005). Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid. Cell Chemistry Biology, 12(5), 595-604. https://doi.org/10.1016/j.chembiol.2005.04.007

Developing small-molecule antagonists against protein-protein interactions will provide powerful tools for mechanistic/functional studies and the discovery of new antibacterials. We have developed a reverse yeast three-hybrid approach that allows hig... Read More about Discovery of antagonist peptides against bacterial helicase-primase interaction in B. stearothermophilus by reverse yeast three-hybrid.

DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings (2004)
Journal Article
Thirlway, J., Turner, I. J., Gibson, C. T., Gardiner, L., Brady, K., Allen, S., …Soultanas, P. (2004). DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings. Nucleic Acids Research, 32(10),

Loading of the replicative ring helicase onto the origin of replication (oriC) is the final outcome of a well coordinated series of events that collectively constitute a primosomal cascade. Once the ring helicase is loaded, it recruits the primase an... Read More about DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings.