The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth

Gunn, Laura H.; Avila, Elena Martin; Birch, Rosemary; Whitney, Spencer M.

doi:10.1073/pnas.2011641117

Cited by 38 publications

(45 citation statements)

References 51 publications

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“…2018 ). Thus, together these results indicate that rubisco kinetic traits are perhaps not as inextricably linked as originally thought, and suggest that there is scope for increasing the catalytic efficiency of the enzyme as has happened in nature for rubisco in some red algae ( Andersson and Backlund 2008 ; Gunn et al. 2020 ).…”

Section: Introductionmentioning

confidence: 67%

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off

Bouvier

Emms

Rhodes

et al. 2021

Molecular Biology and Evolution

127

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Rubisco assimilates CO2 to form the sugars that fuel life on earth. Correlations between rubisco kinetic traits across species have led to the proposition that rubisco adaptation is highly constrained by catalytic trade-offs. However, these analyses did not consider the phylogenetic context of the enzymes that were analysed. Thus, it is possible that the correlations observed were an artefact of the presence of phylogenetic signal in rubisco kinetics and the phylogenetic relationship between the species that were sampled. Here, we conducted a phylogenetically-resolved analysis of rubisco kinetics and show that there is a significant phylogenetic signal in rubisco kinetic traits. We re-evaluated the extent of catalytic trade-offs accounting for this phylogenetic signal and found that all were attenuated. Following phylogenetic correction, the largest catalytic trade-offs were observed between the Michaelis constant for CO2 and carboxylase turnover (∼21-37%), and between the Michaelis constants for CO2 and O2 (∼9-19%), respectively. All other catalytic trade-offs were substantially attenuated such that they were marginal (<9%) or non-significant. This phylogenetically resolved analysis of rubisco kinetic evolution also identified kinetic changes that occur concomitant with the evolution of C4 photosynthesis. Finally, we show that phylogenetic constraints have played a larger role than catalytic trade-offs in limiting the evolution of rubisco kinetics. Thus, although there is strong evidence for some catalytic trade-offs, rubisco adaptation has been more limited by phylogenetic constraint than by the combined action of all such trade-offs.

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Section: Introductionmentioning

confidence: 67%

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off

Bouvier

Emms

Rhodes

et al. 2021

Molecular Biology and Evolution

127

View full text Add to dashboard Cite

show abstract

“…The unique phenotype of the AncIB strain could be a direct result of the ancestral RbcL subunit or due to impediments to the assembly and activationof a hexadecamer RuBisCO complex containing both the ancestral RbcL and modern RbcS subunits. Another possibility is hampered integration of ancestral RbcL given a modern suite of associated proteins required for RuBisCO folding and assembly (57). Further, while overexpression of the ancestral RbcL occurred at the level of transcription and translation, the ancestral strain appears to have comparable levels of assembled hexadecamer RuBisCO, suggesting lower rates of RuBisCO assembly (or faster degradation).…”

Section: Discussionmentioning

confidence: 99%

Resurrected Rubisco suggests uniform carbon isotope signatures over geologic time

Kędzior

et al. 2021

Preprint

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Uniformitarian assumptions underlie the oldest evidence for living organisms on Earth, the distinct isotope fractionation between inorganic and organic carbon. Aside from a handful of compelling deviations, the 13C/12C isotopic mean of preserved organic carbon (δ13Corg) has remained remarkably unchanged through time. RuBisCO is the principal carboxylase/oxygenase biomolecular component that is thought to primarily account for the generation of these distinct carbon isotopic signals. However, it is difficult to reconcile a mostly unchanging mean δ13Corg with several known factors that can affect the isotope fractionation of RuBisCO, such as atmospheric composition and the amino acid composition of the enzyme itself, which have each changed markedly over Earth history. Here we report the resurrection and genetic incorporation of a Precambrian-age, Form IB RuBisCO in a modern cyanobacterial host. The isotopic composition of biomass relative to CO2 (ϵp) in ancestral and control strains were much greater when grown under Precambrian CO2 concentrations compared to modern ambient levels, but displaying values within a nominal envelope of modern-day RuBisCO IB enzyme variants. We infer that these isotopic differences derive indirectly from the decreased fitness of the AncIB strain, which includes diminished growth capacity and total cell RuBisCO activity. We argue that to answer the greatest questions of deep-time paleobiology, ancient biogeochemical signals should be reproduced in the laboratory through the synthesis of the geologic record with experimentally-derived constraints on underlying ancient molecular biology.

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“…Finally, an updated examination of rubisco kinetics in the context of other enzymes has shown that it is not as inefficient a catalyst as often assumed (Bathellier et al ., 2018). Thus, together these results indicate that rubisco kinetic traits are perhaps not as inextricably linked as originally thought, and suggest that there is scope for increasing the catalytic efficiency of the enzyme as has happened in nature for rubisco in some red algae (Andersson and Backlund, 2008; Gunn et al ., 2020).…”

Section: Introductionmentioning

confidence: 69%

Rubisco adaptation is more limited by phylogenetic constraint than by catalytic trade-off

Emms

Rhodes

et al. 2020

Preprint

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RuBisCO assimilates CO2 to form the sugars that fuel life on earth. Correlations between RuBisCO kinetic traits across species have led to the proposition that RuBisCO adaptation is constrained by catalytic trade-offs. However, these correlations were founded on the assumption that kinetic measurements in different species are independent. Here, we show that this assumption is incorrect in angiosperms by evaluating the dependence of variation in RuBisCO kinetic traits on the phylogenetic tree that relates the enzymes. We show that there is significant phylogenetic signal in all carboxylase kinetic traits in angiosperms, and significant phylogenetic signal in the Michaelis constant for O2 in species that conduct C3 photosynthesis. When accounting for this non-independence, we show that the catalytic trade-off between carboxylase turnover and the Michaelis constant for CO2 is weak (∼30 % dependency) and that the correlations between all other RuBisCO kinetic traits are either not-significant or marginal (<9 % dependency). Finally, we demonstrate that phylogenetic constraints limit RuBisCO adaptation to a greater extent than catalytic trade-offs. Thus, the biochemical landscape of RuBisCO adaptation in angiosperms is predominantly limited by phylogenetic constraint and a partial trade-off between carboxylase turnover and the Michaelis constant for CO2.

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The dependency of red Rubisco on its cognate activase for enhancing plant photosynthesis and growth

Cited by 38 publications

References 51 publications

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off

Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off

Resurrected Rubisco suggests uniform carbon isotope signatures over geologic time

Rubisco adaptation is more limited by phylogenetic constraint than by catalytic trade-off

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