Ubiquitin is conjugated to target proteins via isopeptide bonds, a very stable linkage that can be retained within a large range of pH and temperatures. However, a stream of recent literature has identified several eukaryotic ubiquitin enzymes (E3 ligases) that promote ubiquitylation on residues such as threonine, serine and on bacterial lipopolysaccharides (non-canonical ubiquitylation). The ester bond formed between ubiquitin and threonine/serine or lipopolysaccharides is more chemically labile than the isopeptide bond. Therefore, ubiquitylation events built upon ester bonds are often missed as they are not retained during standard sample preparation procedures because of their labile nature. Appropriate mass spectrometry methods are urgently needed to accurately detect and quantify non-canonical ubiquitylation events in complex biological samples.
The aim of this project is to develop both targeted and non-targeted mass spectrometry tools to detect non-canonical ubiquitylation events in complex matrices, to study the molecular mechanisms involved in their formation as well as their biological role.
Applicants are expected to hold (or be about to achieve) at least a 2:1 Honours degree in a relevant subject or demonstrably equivalent experience.
This studentship is funded by the EN & MN Lindsay Scholarship. The 4-year studentship comes with a stipend of £17,668k per annum plus generous research funds of £5,000 per annum.
Applications are open to candidates classed as Home and Rest of UK (RUK) / Channel Islands or Isle of Man students. This includes UK, EU and Irish Nationals who meet the residency requirements of the University, please see here for more information. Please check the requirements carefully to ensure you qualify.
Please note the deadline for applications is Monday 20th February 2023. Please note there are two projects advertised for this studentship, with only one studentship available.
To apply - please visit our website - https://dundee.onlinesurveys.ac.uk/en-mn-lindsay-scholarship-2023-entry