Laura Gunn

In the Gunn lab we study and engineer nature’s vital, but notoriously inefficient, CO2-fixing enzyme, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), whose catalysis often limits the growth and yield of crop plants.

We look for ways to develop the prerequisite information and tools to express more efficient Rubisco variants in synthetic biology systems and in crops: by identifying unique structure-function, overcoming chaperone incompatibilities, and understanding and utilizing the catalytic influence of the auxiliary Rubisco small subunit.

Select journal articles:

• Gunn, L.H., Avila, E.M., Birch, R., and Whitney, S.M. (2020). The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth. Proc. Natl. Acad. Sci. 117, 25890-2589. 
• Bielecki, J., Hantke, M.F., Daurer, B.J., Reddy, H.K.N., Hasse, D., Larsson, D.S.D., Gunn, L.H., Svenda, M., Munke, A., Sellberg, J.A., et al. (2019). Electrospray sample injection for single-particle imaging with X-ray lasers. Science Advances 5:eaav8801.  
• Valegård, K., Hasse, D., Andersson, I., and Gunn, L.H. (2018). Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphate. Acta Crystallogr. D 74, 1-9.
• Gunn, L.H., Valegård, K., and Andersson, I. (2017). A Unique Structural Domain in Methanococcoides burtonii Rubisco Acts as a Small-subunit Mimic. J. Biol. Chem. jbc.M116.767145. 
• Okamoto, K., Miyazaki, N., Larsson, D.S.D., Kobayashi, D., Svenda, M., Mühlig, K., Maia, F.R.N.C., Gunn, L.H., Isawa, H., Kobayashi, M., et al. (2016). The infectious particle of insect-borne totivirus-like Omono River virus has raised ridges and lacks fibre complexes. Sci. Rep. 6, 33170. 
• Sharwood, R.E., Ghannoum, O., Kapralov, M.V., Gunn, L.H., and Whitney, S.M. (2016). Temperature responses of Rubisco from Paniceae grasses provide opportunities for improving C3 photosynthesis. Nat. Plants 2, 16186.