Protein kinase G activation by transmembrane signalling

We have identified a transmembrane complex that senses external amino acids and activates PknG in response to this stimulus.

This project will focus on structural determination of PknG with its activation complex to understand the mechanism of kinase activation, and to compare this signalling system between pathogens and non-pathogens.

Techniques that will be undertaken during the project

• Protein structure determination by electron microscopy (Cryo-EM) and X-ray crystallography
• Membrane protein biochemistry
• Protein biophysical techniques to measure size, folding and interactions (including mass photometry, biolayer interferometry, intrinsic fluorescence)
• Molecular techniques: gene cloning, mutagenesis, genetic modification of bacteria for recombinant protein production and for phenotypic assay (gene knockout)
• Protein kinase assays

Enquiries

Project Enquiries to hmo7@leicester.ac.uk

Programme enquiries to mibtp-admin@leicester.ac.uk

To apply please refer to

https://le.ac.uk/study/research-degrees/funded-opportunities/bbsrc-mibtp

Funding Notes

All MIBTP students will be provided with a 4 year studentship. This includes: Tuition fees at the UK fee rate*, a tax free stipend which for 2026/7 is £21,805 per year (2027/8 stipend to be confirmed), a travel allowance over years 1-3, a travel/conference budget, a generous consumables budget, use of a laptop for the duration of the programme. The University of Leicester will provide full overseas fee waivers for the duration of their study to all international students accepted at Leicester. The funder, UKRI, allows us to appoint up to 30% overseas students.

References

An Aspartate-Specific Solute-Binding Protein Regulates Protein Kinase G Activity To Control Glutamate Metabolism in Mycobacteria (Bhattacharyya et al 2018) doi: 10.1128/mBio.00931-18.

Characterisation of the conformational changes of GlnH that stimulate PknG activity in Mycobacteria and Corynebacterium glutamicum (Tompkins et al 2026) https://doi.org/10.64898/2026.07.02.735984