Outputs (7)

The intracellular immune receptor Rx1 regulates the DNA-binding activity of a Golden2-like transcription factor (2017)
Journal Article
Townsend, P., Dixon, C., Slootweg, E., Sukarta, O., Yang, A., Hughes, T., …Cann, M. (2018). The intracellular immune receptor Rx1 regulates the DNA-binding activity of a Golden2-like transcription factor. Journal of Biological Chemistry, 293(9), 3218-3233. https://doi.org/10.1074/jbc.ra117.000485

Plant NLR proteins enable the immune system to recognise and respond to pathogen attack. An early consequence of immune activation is transcriptional reprogramming and some NLRs have been shown to act in the nucleus and interact with transcription fa... Read More about The intracellular immune receptor Rx1 regulates the DNA-binding activity of a Golden2-like transcription factor.

The tomato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor I-2 couples DNA-Binding to Nucleotide-Binding Domain Nucleotide Exchange (2015)
Journal Article
Fenyk, S., Dixon, C. H., Kittens, W. H., Townsend, P. D., Sharples, G. .., Pålsson, L. .-O., Takken, F. L. W., & Cann, M. J. (2016). The tomato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor I-2 couples DNA-Binding to Nucleotide-Binding Domain Nucleotide Exchange. Journal of Biological Chemistry, 291(3), 1137-1147. https://doi.org/10.1074/jbc.m115.698589

Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable plants to recognise and respond to pathogen attack. Previously, we demonstrated that the Rx1 NLR of potato is able to bind and bend DNA in vitro. DNA binding in situ requires its genu... Read More about The tomato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor I-2 couples DNA-Binding to Nucleotide-Binding Domain Nucleotide Exchange.

The Potato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor Rx1 is a Pathogen Dependent DNA-Deforming Protein (2015)
Journal Article
Fenyk, S., Townsend, P. D., Dixon, C. H., Spies, G. B., de San Eustaquio Campillo, A., Slootweg, E. J., …Cann, M. J. (2015). The Potato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor Rx1 is a Pathogen Dependent DNA-Deforming Protein. Journal of Biological Chemistry, 290(41), 24945-24960. https://doi.org/10.1074/jbc.m115.672121

Plant NLR proteins enable cells to respond to pathogen attack. Several NLRs act in the nucleus, however, conserved nuclear targets that support their role in immunity are unknown. Previously we noted a structural homology between the NB domain of NLR... Read More about The Potato Nucleotide-Binding Leucine-Rich Repeat (NLR) Immune Receptor Rx1 is a Pathogen Dependent DNA-Deforming Protein.

The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein (2015)
Journal Article
Townsend, P., Rodgers, T., Glover, L., Korhonen, H., Richards, S., Colwell, L., …Cann, M. (2015). The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein. Journal of Biological Chemistry, 290(36), 22225-22235. https://doi.org/10.1074/jbc.m115.669267

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. Both experimental and theoretical evidence demonstrate that allostery can be communicated through altered slow relaxation protein dynamics... Read More about The role of protein-ligand contacts in allosteric regulation of the Escherichia coli Catabolite Activator Protein.

Global low-frequency motions in protein allostery: CAP as a model system (2015)
Journal Article
Townsend, P., Rogers, T., Pohl, E., Wilson, M., McLeish, T., & Cann, M. (2015). Global low-frequency motions in protein allostery: CAP as a model system. Biophysical Reviews, 7(2), 175-182. https://doi.org/10.1007/s12551-015-0163-9

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformation... Read More about Global low-frequency motions in protein allostery: CAP as a model system.

The crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factors (2014)
Journal Article
Townsend, P., Jungwirth, B., Pojer, P., Bußmann, M., Money, V., Cole, S., …Pohl, E. (2014). The crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factors. PLoS ONE, 9(12), Article e113265. https://doi.org/10.1371/journal.pone.0113265

The cyclic AMP-dependent transcriptional regulator GlxR from Corynebacterium glutamicum is a member of the super-family of CRP/FNR (cyclic AMP receptor protein/fumarate and nitrate reduction regulator) transcriptional regulators that play central rol... Read More about The crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factors.

A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice (2012)
Journal Article
Fenyk, S., de San Eustaquio Campillo, A., Pohl, E., Hussey, P., & Cann, M. (2012). A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice. Journal of Biological Chemistry, 287(6), 4023-4032. https://doi.org/10.1074/jbc.m111.314450

Plant resistance proteins (R-proteins) are key components of the plant immune system activated in response to a plethora of different pathogens. R-proteins are P-loop NTPase superfamily members, and current models describe their main function as ATPa... Read More about A Nucleotide Phosphatase Activity in the Nucleotide Binding Domain of an Orphan Resistance Protein from Rice.