Condensation of Rubisco into a proto-pyrenoid in higher plant chloroplasts.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 33298923.
- Also identified by DOI 10.1038/s41467-020-20132-0 and PMC identifier 7726157.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Photosynthetic CO<sub>2</sub> fixation in plants is limited by the inefficiency of the CO<sub>2</sub>-assimilating enzyme Rubisco. In most eukaryotic algae, Rubisco aggregates within a microcompartment known as the pyrenoid, in association with a CO<sub>2</sub>-concentrating mechanism that improves photosynthetic operating efficiency under conditions of low inorganic carbon. Recent work has shown that the pyrenoid matrix is a phase-separated, liquid-like condensate. In the alga Chlamydomonas reinhardtii, condensation is mediated by two components: Rubisco and the linker protein EPYC1 (Essential Pyrenoid Component 1). Here, we show that expression of mature EPYC1 and a plant-algal hybrid Rubisco leads to spontaneous condensation of Rubisco into a single phase-separated compartment in Arabidopsis chloroplasts, with liquid-like properties similar to a pyrenoid matrix. This work represents a significant initial step towards enhancing photosynthesis in higher plants by introducing an algal CO<sub>2</sub>-concentrating mechanism, which is predicted to significantly increase the efficiency of photosynthetic CO<sub>2</sub> uptake.
Medical subject headings
- Arabidopsis
- Chloroplasts
- Plant Proteins
- Plants, Genetically Modified
- Ribulose-Bisphosphate Carboxylase