Analysis of LLPS in Plant Photosynthesis

Plant communities can regulate plant growth and developmental processes through liquid-liquid phase separation (LLPS). CD BioSciences is committed to studying the emerging role of plant phase separation with the aim to provide comprehensive analytical services to explore LLPS in plant photosynthesis.

Introduction to Biomolecular Condensates in Plant Photosynthesis

LLPS is an important mechanism for biomolecular condensate formation. In photosynthetic plants like cyanobacteria and green algae, they can form CO₂ fixation compartments as biomolecular condensates via LLPS. Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) is a single CO₂ fixing enzyme that leads to the loss of fixed CO₂ during photorespiration. To overcome this challenge, almost all marine photosynthetic autotrophs have evolved different types of CO₂ concentration mechanisms (CCM) to inhibit photorespiration and enhance CO₂ fixation. In cyanobacterial CCM, Rubisco and carbonic anhydrase are isolated in the carboxysome, while in eukaryotic green algal CCM, Rubisco is in the nucleoprotein matrix. Both carboxysomes and nucleoprotein matrices are membrane-free phase-separated compartments.

Fig. 1. The proteins and interactions that underlie Rubisco condensates. (Wunder T, et al., 2020)

Customized Services

Understanding the complex mechanisms involved in photosynthesis is essential for improving agricultural productivity and developing sustainable energy sources. CD BioSciences offers professional services to analyze LLPS in plant photosynthesis, aiming to help clients understand the role of LLPS in the formation of Rubisco condensates. Our strategies are as follows:

(1) One of the key approaches used by CD BioSciences is the combination of biochemical recombination with structural biology. This powerful combination allows us to reconstruct and visualize the formation of Rubisco condensates, such as carboxysomes in amoebae and nucleoproteins in microalgae, and their role in enhancing enzyme efficiency and CO2 specificity assimilation.

(2) By purifying and reconstituting Rubisco complexes in vitro, we are able to analyze the structures of three Rubisco-linked scaffold proteins, their adhesions and spacer regions, and their role in condensate formation. Our structural studies, including X-ray crystallography and cryo-electron microscopy, can provide high-resolution insight into the spatial organization of Rubisco condensates and help identify key protein-protein and protein-RNA interactions.

(3) We can also perform detailed in vitro and in vivo characterization of Rubisco condensates to analyze the role of LLPS. The behavior of Rubisco condensates and candidate scaffolds for fluorescent fusion proteins in vivo is also examined.

(4) LLPS on carboxysomes and nuclear proteins provide key information for engineering algal CCM into crop plants to improve photosynthetic efficiency. Our experts are committed to introducing prokaryotic and eukaryotic CCM into higher plants based on phase-separated scaffold proteins.

CD BioSciences is at the forefront of groundbreaking discoveries in plant biology with its expertise in LLPS analysis and advanced analytical services. By leveraging our integrated analytical approach, researchers can gain unprecedented insight into the formation, function, and regulation of LLPS-driven condensates in plant photosynthesis, paving the way for increased agricultural productivity and sustainable energy solutions. If you have any special requirements for our services, please feel free to contact us.