© The Author(s) 2019. The chloroplast pyrenoid, an important component of the CO2 concentrating mechanism of algae, is a structure composed primarily of Rubisco. In Chlamydomonas, Rubisco in the pyrenoid is held together by the linker protein EPYC1. Atkinson et al., (2019) determined the regions of the Rubisco small subunit and EPYC1 that are important for the protein-protein interaction, thus making progress towards reconstruction of a pyrenoid in higher plants. Why is a protein soluble in one organism while its homologue in another species becomes part of a liquidlike cell structure? That is the question being addressed by Atkinson et al., (2019) in this issue of the Journal of Experimental Botany. It is even more striking when the protein is ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), the most abundant soluble enzyme in plants and algae. In terrestrial plants, Rubisco behaves as a soluble protein found throughout the chloroplast stroma of leaf mesophyll cells. However, in most algae, Rubisco is found in a structure within the chloroplast called the pyrenoid.
Publication Source (Journal or Book title)
Journal of Experimental Botany
Mukherjee, A., & Moroney, J. (2019). How protein - Protein interactions contribute to pyrenoid formation in Chlamydomonas. Journal of Experimental Botany, 70 (19), 5033-5035. https://doi.org/10.1093/jxb/erz299