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Investigating the roles of novel redox proteins in cellulose degradation


Project Description

Co-supervisor Dr Paul Walton, University of York

We are too heavily dependent upon oil to meet our energy needs. Making better use of waste plant material as an energy source is therefore a key target of modern industrial biotechnology. This means accessing the glucose, which is stored within plant cell walls as cellulose, and converting it to ethanol by fermentation. Cellulose is a highly stable solid and so its break down is a significant challenge. The recent discovery of Lytic Polysaccharide Monooxygenases (LPMOs), enzymes that are able to oxidatively augment the action of glycoside hydrolases in this process, has therefore generated a lot of excitement. Our aim is to further our understanding of the extracellular oxidative processes that are taking place when microbes utilize these enzymes for biomass breakdown.

We have identified a set of bacterial proteins that appear to target cellulose and contain domains with likely redox functions. During your PhD, you will investigate these proteins as potential LPMO activators by expressing and purifying them before performing a full structural and functional analysis of their roles. The knowledge gained from this research will provide new knowledge of the electron transfer processes that underpin the oxidative deconstruction of biomass.

Funding Notes

BBSRC White Rose Mechanistic Biology DTP 4 year studentship.

Studentships covers UK/EU fees and stipend (c.£14,553) for 4 years to start in Oct 2018. Applicants should have/be expecting at least a 2.1 Hons. degree in a relevant subject. EU candidates require 3 years of UK residency in order to receive full studentship.

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process and the projects selected by the successful candidates will be funded.

There are 2 stages to the application process. Please see our website for more information: View Website

References

HEMSWORTH
Frandsen, K. E. H., Simmons, T. J., Dupree, P., Poulsen, J.-C. N., Hemsworth, G. R., Ciano, L., Johnston, E. M., Tovborg, M., Johansen, K. S., Freiesleben, von, P., Marmuse, L., Fort, S., Cottaz, S., Driguez, H., Henrissat, B., Lenfant, N., Tuna, F., Baldansuren, A., Davies, G. J., Leggio, Lo, L., and Walton, P. H. (2016) The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nat Chem Biol. 12, 298–303
Hemsworth, G. R., Johnston, E. M., Davies, G. J., and Walton, P. H. (2015) Lytic Polysaccharide Monooxygenases in Biomass Conversion. Trends Biotechnol. 33, 747–761
Hemsworth, G. R., Henrissat, B., Davies, G. J., and Walton, P. H. (2014) Discovery and characterization of a new family of lytic polysaccharide monooxygenases. Nat Chem Biol. 10, 122–126
Hemsworth, G. R., Taylor, E. J., Kim, R. Q., Gregory, R. C., Lewis, S. J., Turkenburg, J. P., Parkin, A., Davies, G. J., and Walton, P. H. (2013) The copper active site of CBM33 polysaccharide oxygenases. J Am Chem Soc. 135, 6069–6077

BERRY:
Timms, N., Windle, C.L., Polyakova, A., Ault, J.R., Trinh, C.H., Pearson, A., Nelson, A. and Berry, A.(2013) Structural Insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with -thialysine by using a chemical mutagenesis strategy. Chembiochem, 14, 474-481
Pearsall, S.M., Rowley, C.N. and Berry, A. (2015) Advances in pathway engineering for natural product biosynthesis. Chemcatchem dx.doi.org/10.1002/cctc.201500602
Windle, C.L., Simmons, K., Ault, J.R., Trinh, C.H., Nelson, A., Pearson, A.R. and Berry, A. (2017) Extending enzyme molecular recognition with an expanded amino acid alphabet. Proc Natl Acad Sci USA, 114, 2610-2615. DOI:10.1073/pnas.1616816114
Cross, L.L., Paudyal, R., Kamisugi, Y., Berry, A., Cuming, A.C., Baker, A. and Warriner, S.L. (2017) Towards designer organelles by subverting the peroxisomal import pathway. Nature Comms. 8, Article number: 454. Doi: 10.1038/s41467-017-00487-7

WALTON
Frandsen, K. E. H., Simmons, T. J., Dupree, P., Poulsen, J.-C. N., Hemsworth, G. R., Ciano, L., Johnston, E. M., Tovborg, M., Johansen, K. S., Freiesleben, von, P., Marmuse, L., Fort, S., Cottaz, S., Driguez, H., Henrissat, B., Lenfant, N., Tuna, F., Baldansuren, A., Davies, G. J., Leggio, Lo, L., and Walton, P. H. (2016) The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nat Chem Biol. 12, 298–303

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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