Constructing regulatory networks of Rubisco post-translational modifications: a novel avenue for engineering environment adaptive plants.

Chloroplastic proteins play pivotal roles in optimizing photosynthesis, particularly under fluctuating environmental conditions. Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a core enzyme governing plant carbon assimilation and photorespiration. Recent studies have highlighted those post-translational modifications (PTMs), including phosphorylation, acetylation, methylation, and redox Modifications, modulate Rubisco function. These PTMs regulate Rubisco's structural stability, catalytic efficiency, and the plant's photosynthetic acclimation under diverse environmental conditions. However, the upstream enzymes responsible for Rubisco PTMs remain poorly characterized, large due to technical limitations in identifying chloroplast-localized modification events and their associated catalytic components. This review summarizes the latest advances in the types, intrinsic regulatory mechanisms, and associated biological significance of Rubisco PTMs. It further emphasizes the integration of interdisciplinary approaches, including high-throughput photosynthetic phenomics, genomics, high-resolution mass spectrometry, specific immunological antibodies, and artificial intelligence-based molecular dynamics simulations. These integrated strategies are expected to facilitate the construction of PTM regulatory networks of chloroplast proteins, thereby offering guidance for future engineering and modification efforts aimed at developing intelligent environment-adaptive plants.