DESCRIPTION OF LAB RESEARCH WORK
Global biomass production relies on the function of the key photosynthetic enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). Paradoxically, this enzyme is slow and catalyzes a metabolite damaging side-reaction with molecular oxygen. Our laboratory aims to understand how a wide diversity of organisms, such as plants, cyanobacteria and algae, have dealt with the conserved suboptimal properties of this catalyst. Our tools focus on mechanistic biochemistry, with an emphasis on bottom-up reconstitution. We supplement this core expertise with complementary approaches such as structural, cell and molecular biology tools to follow questions of interest.
Currently strong research themes in the group include mechanistic studies of diverse Rubisco activases, molecular motors of the AAA+ ATPase class. We also study the formation of Rubisco containing biomolecular condensates via liquid liquid phase separation, a key strategy of CO2 concentrating mechanisms.
|How Jian Ann
Graduate Research Officer
|Tsai Yi-Chin Candace|
Senior Research Scientist
|Lynette Liew Sin Yee
|Wong Woon Seng|
|Oh Zhen Guo
|Poh Cheng Wei
- Exploration and Utilization of the Natural Diversity of Rubisco Regulators
This project concerns the structural and biochemical characterization of the molecular chaperones known as Rubisco activases (Rca). Three convergently evolved Rca systems have been discovered but function via diverse mechanisms.
- Integrating in vivo and in vitro Approaches for Metagenomic RuBisCO Sequence Mining to Improve Carbon Fixation
In collaboration with the group of Prof. Ron Milo (Weizmann Institute of Science), we are characterizing novel Rubisco enzymes.
- Reconstituting Phase Separations that Enable the Microalgal CO2 Superchargers
Biophysical carbon concentrating mechanisms require Rubisco to be sequestered at high concentration in microcompartments. We are reconstituting these events in vitro, and have found them to be related to the concept of liquid liquid phase separation.
- The Unusual CO2-fixing Engine of Dinoflagellates, the Algae that Powers the Coral Ecosystems
The endosymbionts of corals possess Rubisco enzymes that resemble those of prokaryotes. We are characterizing the structure and biochemistry of these catalysts
- **Tsai YC, Ye F, **Liew L, *Liu D, Bhushan S, Gao YG, Mueller-Cajar O. Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase. Proc Natl Acad Sci U S A. 117(1) 381-387, 2020##
- **Shivhare D, *Ng, J, **Tsai YC, Mueller-Cajar O. Probing the rice Rubisco-Rubisco activase interaction via subunit heterooligomerization. Proc Natl Acad Sci U S A. 116(48) 24041-24048, 2019##
- Atkinson N, Velanis CN, **Wunder T, Clarke DJ, Mueller-Cajar O, McCormick AJ. The pyrenoidal linker protein EPYC1 phase separates with hybrid ArabidopsisChlamydomonas Rubisco through interactions with the algal Rubisco small subunit. J Exp Bot 70(19):5271-5285, 2019##
- **Wunder T, *Oh ZG, Mueller-Cajar O. CO2-fixing liquid droplets: Towards a dissection of the microalgal pyrenoid. Traffic 20(6):380-389, 2019#
- ·**Wunder T, **Cheng SLH, Lai SK, Li HY, Mueller-Cajar O. The phase separation underlying the pyrenoid-based microalgal Rubisco supercharger. Nat. Commun. 9(1):5076, 2018##
- Bhat JY, Miličić G, Thieulin-Pardo G, Bracher A, Maxwell A, Ciniawsky S, Mueller-Cajar O, Engen JR, Hartl FU, Wendler P, Hayer-Hartl M., Mechanism of Enzyme Repair by the AAA(+) Chaperone Rubisco Activase. Mol Cell. 67(5):744-756, 2017##
- *Liu D, *Ramya RCS, Mueller-Cajar O., Surveying the expanding prokaryotic Rubisco multiverse. FEMS Microbiol Lett. 364(16), 2017
- Mueller-Cajar O., The diverse AAA+ Machines that Repair inhibited Rubisco Active Sites. Front Mol Biosci. 4:31, 2017
- *Shivhare D, Mueller-Cajar O., In vitro characterization of thermostable CAM Rubisco activase reveals a Rubisco interacting surface loop. Plant Physiol. 174(3):1505-1516, 2017##
- *Loganathan N, **Tsai YC, Mueller-Cajar O., Characterization of the heterooligomeric red-type rubisco activase from red algae. Proc Natl Acad Sci U S A. 113(49):14019-14024, 2016##