On January 8, Nature Plants published an online research paper titled "Structure of Chlamydomonas reinhardtii LciA guided the engineering of FNT family proteins to gain bicarbonate transport activity," jointly completed by the research group of Huang Jirong from the School of Life Sciences at Shanghai Normal University and the research group of Zhang Peng from the Center for Excellence in Molecular Plant Sciences at the Chinese Academy of Sciences. The study reveals the substrate selectivity mechanism of the HCO3⁻ transport channel LciA in the CO2 concentrating mechanism (CCM) of Chlamydomonas reinhardtii. Through structure-guided molecular design, the researchers successfully achieved rational modification of HCO3⁻ transport activity, providing core components and molecular strategies for enhancing photosynthetic efficiency in C3 crops by utilizing CCM. Photosynthetic algae have evolved an efficient CO2 concentrating mechanism (CCM) over long-term adaptation, which includes aggregates of the 1,5-bisphosphate ribulose carboxylase/oxygenase (RuBisCo) (such as carboxysomes in cyanobacteria and pyrenoids in Chlamydomonas) and multiple inorganic carbon transport proteins. This research was jointly conducted by Shanghai Normal University and the Center for Excellence in Molecular Plant Sciences at the Chinese Academy of Sciences, with postgraduate student Guo Jiaxin and postdoctoral researcher Yang Zhao as co-first authors. The study was supported by the National Natural Science Foundation of China, the National Key R&D Program, the Chinese Academy of Sciences, and the Shanghai Municipal Science and Technology Commission. The Chinese Academy of Sciences must be translated as Chinese Academy of Sciences.
