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Rubisco is evolving for improved catalytic efficiency and CO₂ assimilation in plants.

ABSTRACT: Rubisco is the primary entry point for carbon into the biosphere. However, rubisco is widely regarded as inefficient leading many to question whether the enzyme can adapt to become a better catalyst. Through a phylogenetic investigation of the molecular and kinetic evolution of Form I rubisco we uncover the evolutionary trajectory of rubisco kinetic evolution in angiosperms. We show that rbcL is among the 1% of slowest-evolving genes and enzymes on Earth, accumulating one nucleotide substitution every 0.9 My and one amino acid mutation every 7.2 My. Despite this, rubisco catalysis has been continually evolving toward improved CO₂/O₂ specificity, carboxylase turnover, and carboxylation efficiency. Consistent with this kinetic adaptation, increased rubisco evolution has led to a concomitant improvement in leaf-level CO₂ assimilation. Thus, rubisco has been slowly but continually evolving toward improved catalytic efficiency and CO₂ assimilation in plants.

SUBMITTER: Bouvier JW

PROVIDER: S-EPMC10945770 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature

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Rubisco is evolving for improved catalytic efficiency and CO<sub>2</sub> assimilation in plants.

Bouvier Jacques W JW Emms David M DM Kelly Steven S

Proceedings of the National Academy of Sciences of the United States of America 20240305 11

Rubisco is the primary entry point for carbon into the biosphere. However, rubisco is widely regarded as inefficient leading many to question whether the enzyme can adapt to become a better catalyst. Through a phylogenetic investigation of the molecular and kinetic evolution of Form I rubisco we uncover the evolutionary trajectory of rubisco kinetic evolution in angiosperms. We show that <i>rbcL</i> is among the 1% of slowest-evolving genes and enzymes on Earth, accumulating one nucleotide subst ...[more]

PMID: 38442173

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Project description:Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a key enzyme responsible for biological CO2 assimilation. RuBisCO can be heterologously expressed in Escherichia coli so that glucose and CO2 are co-metabolized to achieve high mixotrophic metabolite production, where the theoretical yield of mixotrophic metabolite production is 2.4 mol(ethanol + acetate + pyruvate)/molglucose. However, RuBisCO is known for its low kcat and for forming inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates, yet the inhibited form of RuBisCO can be reversed by RuBisCO activase (Rca). In this study, RuBisCO forms I and II were cloned and expressed in Escherichia coli for in situ CO2 recycling, where CO2 produced during glucose fermentation was recycled and co-metabolized with the glucose. In addition, forms I and II RuBisCO activases were co-expressed with RuBisCO in E. coli to determine their in vivo effects on in situ CO2 recycling. Form I RuBisCO activase (Rca1) was co-expressed with form I RuBisCO and form II RuBisCO activase (Rca2) was co-expressed with form II RuBisCO. The results showed that both form I and form II RuBisCO exhibit comparable activities in E. coli and generated similar levels of in situ CO2 recycling. A significant increase in the total metabolite yield from 1.5 ± 0.1 to 2.2 ± 0.1 mol(ethanol + acetate + pyruvate)/molglucose occurred when Rca2 was co-expressed with form II RuBisCO. Meanwhile, the total metabolite yield increased from 1.7 ± 0.1 to 2.0 ± 0.1 mol(ethanol + acetate + pyruvate)/molglucose when Rca1 was co-expressed with form I RuBisCO. This data suggests that both forms I and II RuBisCO are subject to in vivo RuBP inhibition yet can be relieved by the co-expression of Rca. Interestingly, it is suggested that the in vivo RuBP inhibition of form II RuBisCO can be more easily reversed compared to form I. When the catalytic power of RuBisCO is maintained by Rca, the high activity of phosphoribulokinase (Prk) plays an important role in directing glucose to the RuBisCO-based engineered pathway and fermentation yields of 2.1-2.3 mol(ethanol + acetate + pyruvate)/molglucose can be obtained. This study is the first to demonstrate that in vivo RuBP inhibition of RuBisCO can be a bottleneck for in situ CO2 recycling in E. coli.

Dataset Information

Rubisco is evolving for improved catalytic efficiency and CO₂ assimilation in plants.

Publications

Rubisco is evolving for improved catalytic efficiency and CO<sub>2</sub> assimilation in plants.

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Dataset Information

Rubisco is evolving for improved catalytic efficiency and CO2 assimilation in plants.

Publications

Rubisco is evolving for improved catalytic efficiency and CO<sub>2</sub> assimilation in plants.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Rubisco is evolving for improved catalytic efficiency and CO₂ assimilation in plants.