A PhD studentship is available to work in the laboratory of Prof. Sasi (Maria R) Conte (https://www.kcl.ac.uk/people/sasi-conte
), in the Randall Centre for Cell and Molecular Biophysics, King’s College London (https://www.kcl.ac.uk/lsm/research/divisions/randall
). The successful applicant will be joining a dynamic, interdisciplinary and internationally renowned lab, within one of the world’s top research universities. We are seeking a highly motivated and enthusiastic candidate with background in structural biology/biochemistry/chemistry/biophysics and a strong interest in molecular mechanisms.
The laboratory of Prof. Conte is interested in investigating the role and mechanism of RNA-binding proteins. Protein-RNA interactions control the fate of all RNA molecules in the cell thereby playing a central role in regulating gene expression at post-transcriptional level. Perturbations in these interactions are common features in many diseases including cancer, neurodegeneration and metabolic disorder. We are particularly interested in a superfamily of RNA binding proteins called La-related proteins (LARPs), that have recently emerged as crucial regulator of gene expression at post-transcriptional level, playing key roles in cancer biology and other diseases. Our recent studies have shown that one of the LARPs, namely LARP4A, interacts with RNA using intrinsically disordered regions that do not contain any recognisable RNA binding domain or motif (Nucleic Acids Research, 2019), thus revealing a novel RNA recognition mechanism. Moreover, we established that LARP4A-RNA interaction is modulated by an interplay with the PolyA binding protein. As LARP4A has a role in cancer cell migration and invasion, investigations in molecular mechanism will elucidate how translational circuitries are affected in cancer cells.
This exciting PhD position will investigate the detailed mechanism of recognition between LARPs and their RNA and protein partners. To achieve this, the student will use molecular biology, protein biochemistry, a wide range of biophysical and biochemical methodologies (NMR, X-ray, SAXS, ITC, EMSA etc.). The student will be also working closely with interdisciplinary collaborators to test hypotheses in the context of cancer cells and model organisms. For further information, please find our previously reported findings from the reference section below.
Student profile: Prospective candidates should have a 1st or 2:1 M-level qualification in Biochemistry, Chemistry, Biophysics or a related programme, in which all aspects of basic chemical knowledge have been covered. Preference will be given to those with a good knowledge on analytical techniques and/or structural and molecular biology methods including NMR and protein expression and purification. The ideal candidate will be passionate about biology, motivated, organized and hard working with a ‘can do’ attitude. All applicants should indicate in their applications how they intend to fund their studies. We prefer candidates that have secured or wish to secure their own competitive funding.
The selected candidate will extensively use structural biology, biochemistry and molecular biology to address the above questions. In addition, the candidate will be exposed to state-of-the-art facilities including the centre for Biomolecular Spectroscopy at King’s, of which Conte is Director. King’s College London is amongst the top 30 universities in the World and has an established PhD programme. It provides support with high-quality training and career development activities which includes development of skills essential for career progression such as presentation and writing skills. This combination is likely to be highly sought after by future employers and funders. The student will be based in the Randall Centre, School of Basic and medical Biosciences which provides an exciting training environment.
To apply, please send all the following documents to Prof. Sasi Conte ([email protected]
• Detailed CV
• Details of 2 academic referees with email contacts
• All degree certificates and transcripts (Undergraduate AND Postgraduate MSc-officially translated into English where necessary)
• A research statement (max. 1.5 pages) describing why you are suitable for this PhD studentship
• A statement of how they intend to fund their studies
Incomplete applications will not be considered.
Only self-funded students are eligible. There is no funding attached to this PhD call and the successful applicant will be expected to provide the funding for Tuition fees, living expenses and maintenance. Additional Research Costs between £7,000-12,000 per annum are required for consumables.
Applicants should indicate in their applications how they intend to fund their studies. We prefer candidates that have secured or wish to secure their own competitive funding from overseas government agencies or employers for example:
Other scholarships are available from the China-Scholarship Council (CSC).
Applicants are required to meet King’s English language requirements (Band D, View Website).
Cruz-Gallardo, I., Martino, L., Kelly, G., Atkinson, A., Trotta, R., De Tito, S., Coleman, P., Ahdash, Z., Gu, Y., Bui, T.TT Conte, M.R.* (2019) LARP4A recognises polyA RNA via a novel binding mechanism mediated by disordered regions and involving the PAM2w motif, revealing interplay between PABP, LARP4A and mRNA. Nucleic Acids Res., Epub, doi: 10.1093/nar/gkz144. Recommended by F1000
Maraia, R.J.*, Mattijssen, S., Cruz-Gallardo, I., Conte, M.R.* (2017) The La and related RNA-binding proteins (LARPs): structures, functions, and evolving perspectives. Wiley Interdiscip Rev RNA. 8(6) doi: 10.1002/wrna.1430.
Seetharaman, S., Flemying, E., Shen, J., Conte, M.R., Ridley, A.E. (2016) The RNA-binding protein LARP4 regulates cancer cell migration and invasion, Cytoskeleton, 73, 680-690.
Martino, L., Pennell, S., Kelly, G., Busi, B., Brown, P., Atkinson, R.A., Salisbury, N.J.H., Ooi, Z-H., See, K-W., Smerdon, S.J., Alfano, C., Bui, T.T., Conte, M.R.* (2015) Synergic interplay of the La motif, RRM1, and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module. Nucleic Acids Res, 43, 645-60.
How good is research at King’s College London in Biological Sciences?
FTE Category A staff submitted: 73.85
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