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Biology subjects

Capo-Bauca, S.

Publications and source records attributed to Capo-Bauca, S..

2 recordsLinked to original sources

Diversity in Rubisco Kinetics and CO2-Concentrating Mechanisms Among Cyanobacterial Lineages

Cyanobacteria are the most ancient oxygenic photosynthetic organisms on Earth and play a pivotal role in the global carbon cycle. Despite their ecological and evolutionary significance, the mechanisms of carbon acquisition and fixation in this phylum remain largely unexplored beyond a few model species. Here, we examined representative taxa spanning the full phylogenetic breadth of Cyanobacteria, assessing in vivo carbon-acquisition pathways, the role and efectiveness of CO2-concentrating mechanisms (CCMs), as well as conducting in vitro biochemical characterizations of the kinetic traits and carbon isotope fractionation of Rubisco. We found significant lineage-specific diferences in Rubisco kinetics and CCM performance, but a common signature of high Rubisco catalytic turnover coupled with low CO2 afinity--consistent with the co-evolution of this enzyme together with powerful CCMs. Furthermore, we identified a strong positive correlation between Rubisco carbon isotope fractionation and its CO2/O2 specificity factor. Together, these results provide fresh insight into Rubisco catalysis and shed light on its co-evolution with CCMs, underscoring their role in shaping Earths carbon dynamics.

plant biology↗

The fitness landscape of a Form II Rubisco in a photosynthetic bacterium guides engineering of oxygen tolerance

Rubisco is an important but challenging protein engineering target. Fast and selective rubiscos could enhance photosynthesis in plants and accelerate biobased production processes. To facilitate engineering of rubisco, we applied an in vivo screen that couples rubisco activity to growth rate of the photoautotrophic cyanobacterium Synechocystis sp. PCC 6803. We screened a barcoded mutagenesis library of the form II rubisco from Gallionella sp. containing 15,000 single-site and multi-site variants. Exchanges in loop 6 near the active site, at the dimer interface, and in potential gas tunnels improved rubisco fitness. The dataset also informed protein engineering, using recombination and a trained transformer model. In vitro characterisation of two high-fitness variants showed reduced catalytic efficiency for oxygenation (kcat/Ko) in both and an increased carboxylation turnover (kcatC) in one. This large labeled fitness dataset, containing examples of epistasis, can be useful for benchmarking computational models of rubisco. TeaserEvolving a foreign rubisco to photosynthesis leads to reduced oxygen sensitivity.

biochemistry↗