Gunn lab
We study and engineer nature’s vital, but notoriously inefficient CO2-fixing enzyme, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), whose catalysis limits the growth of crop plants and cyanobacteria used for biofuel production.We look for ways to develop the prerequisite information and tools to express more efficient Rubisco variants in crops and cyanobacteria: by identifying unique structure-function, overcoming chaperone incompatibilities, and understanding and utilizing the catalytic influence of the auxiliary Rubisco small subunit.
Popular science presentation
Watch our "2 minute" popular science presentation on youtube for an easily accessible introduction to our research.
Read more about expressing red Rubsico in Green Plants here and here.
Research projects
We combine evolutionary, computational, sequence-structure-function (x-ray crystallography, serial-femtosecond crystallography), biochemistry, and synthetic biology approaches to address our research questions.
Weird Rubiscos
Rubisco isoforms can be found in a diverse range of phylogenetically distinct organisms, including leafy green plants, algae, bacteria, and even archaea. These different Rubisco isoforms have evolved under very different selection pressures, and may exhibit “weird” kinetics, assembly pathways, thermotolerance, or other strange properties. We look for exotic Rubisco sequence-structure, in order to harness unique and beneficial CO2-fixing strategies.
Red Rubisco
The structure and function of “red” Rubiscos found in red algae and diatoms diverges from that of “green” Rubiscos found in leafy plants. Red Rubiscos are much more efficient than green Rubiscos, but the reason for their remarkable kinetics is unknown. We aim to harness naturally superior red Rubisco kinetics, using structural biology, protein engineering and synthetic biology approaches.
Green Rubisco
Higher plants (with “green” Rubiscos) contain auxiliary subunits called “small” subunits. Plants contain multiple small subunit isoforms, which are differentially expressed in response to a variety of environmental cues. This project aims to characterise and take advantage of the contribution of different auxiliary subunits to Rubisco assembly and activity.
Computational studies
We use Molecular Dynamics simulations to identify sequence-structure that channels the correct substrate to the active site in Rubisco. Molecular Dynamics analysis of a diverse range of Rubiscos from different evolutionary lineages will be combined with sequence-structure information to identify amino acids that contribute to enhanced substrate selectivity.
Publications
Observation of a single protein by ultrafast X-ray diffraction
Part of Light, 2024
Twelve new metagenome-assembled genomes from non-axenic culture of Griffithsia monilis (Rhodophyta)
Part of Microbiology Resource Announcements, p. 1-5, 2024
Grafting Rhodobacter sphaeroides with red algae Rubisco to accelerate catalysis and plant growth
Part of NATURE PLANTS, p. 978-986, 2023
Red Rubiscos and opportunities for engineering green plants
Part of Journal of Experimental Botany, p. 520-542, 2022
The small subunit of Rubisco and its potential as an engineering target
Part of Journal of Experimental Botany, p. 543-561, 2022
The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth
Part of Proceedings of the National Academy of Sciences of the United States of America, p. 25890-25896, 2020
Electrospray sample injection for single-particle imaging with x-ray lasers
Part of Science Advances, 2019
Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphate
Part of Acta Crystallographica Section D, p. 1-9, 2018
Part of Journal of Biological Chemistry, p. 6838-6850, 2017
- DOI for A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphatecarboxylase/oxygenase (Rubisco) acts as a small subunit mimic
- Download full text (pdf) of A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphatecarboxylase/oxygenase (Rubisco) acts as a small subunit mimic
Part of Nature Plants, 2016
Part of Scientific Reports, 2016
People
Laura Gunn, PhD
Group Leader
Afshan Begum, PhD
Researcher
Former members
Stavros Azinas, PhD
Postdoctoral researcher
Frida Boström, Masters student
Shruti Ravi, masters student
Natalia Reynisdottir, intern
- Estelle Pignon, masters student
- Ivo van den Hurk, intern
- Celia da Luz, masters student
- Josefin Ågren, intern
- Sara Rönnblad-Ericsson, intern
- Pushkar Chitale, masters student