Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells

Maheshwari, Chirag; Coe, Robert A.; Karki, Shanta; Covshoff, Sarah; Tapia, Ronald; Tyagi, Aruna; Hibberd, Julian M.; Furbank, Robert T.; Quick, W. Paul; Lin, Hsiang-Chun

doi:10.1016/j.jplph.2021.153395

Cited by 11 publications

(6 citation statements)

References 32 publications

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“…The “FvCB model” of photosynthesis ( 114 ), as well as a suite of other experimental ( 115 – 122 ) and computational ( 123 , 124 ) studies all demonstrate that rubisco is a major rate-limiting factor for CO 2 assimilation under ambient steady-state conditions. The findings presented here link these mechanistic studies with evolutionary biology, and reveal that rubisco has experienced directional selection to improve kinetic efficiency and CO 2 assimilation.…”

Section: Discussionmentioning

confidence: 98%

Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Bouvier,

Emms,

Kelly

2024

Proc. Natl. Acad. Sci. U.S.A.

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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 CO 2 /O 2 specificity, carboxylase turnover, and carboxylation efficiency. Consistent with this kinetic adaptation, increased rubisco evolution has led to a concomitant improvement in leaf-level CO 2 assimilation. Thus, rubisco has been slowly but continually evolving toward improved catalytic efficiency and CO 2 assimilation in plants.

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Section: Discussionmentioning

confidence: 98%

Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Bouvier,

Emms,

Kelly

2024

Proc. Natl. Acad. Sci. U.S.A.

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“…The 'FvCB model' of photosynthesis 113 , as well as a suite of other experimental [114][115][116][117][118][119][120][121] and computational 122,123 studies all demonstrate that rubisco is a major rate-limiting factor for CO2 assimilation under ambient steady-state conditions. The findings presented here link these mechanistic studies with evolutionary biology, and reveal that rubisco has experienced directional selection to improve kinetic efficiency and CO2 assimilation.…”

Section: Discussionmentioning

confidence: 98%

Rubisco is evolving for improved catalytic efficiency and CO₂assimilation in plants

Bouvier

Emms

Kelly

2022

Preprint

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Rubisco assimilates CO2 to form the sugars that fuel life on Earth. Although rubisco is the source of most carbon in the biosphere, it is a surprisingly inefficient catalyst with a modest carboxylase turnover rate and a competing oxygenase activity which results in the loss of fixed CO2. These apparent shortcomings of rubisco present a puzzling evolutionary paradox: why does the enzyme appear well suited to the high CO2 low O2 conditions of its origin, rather than the low CO2 high O2 conditions of the present day? To help answer this question, we perform a phylogenetically resolved analysis of the molecular and kinetic evolution of Form I rubisco. We discover that rubisco is among the slowest evolving genes on Earth. Specifically, we find that the rubisco catalytic large subunit evolves substantially slower than its cognate small subunit, and is slower than >98% of all other genes and enzymes across the tree of life. Next, through simultaneous analysis of rubisco molecular and kinetic evolution in C3 angiosperms, we demonstrate that despite its slow molecular evolution, rubisco kinetics have evolved, and are continuing to evolve, to improve CO2/O2 specificity, carboxylase turnover and overall carboxylation efficiency. Thus, slow molecular evolution has severely limited rubisco kinetic optimisation, resulting in the present enzyme that is poorly adapted for current conditions.

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“…Rubisco is the key enzyme of carbon fixation in plant, and improving Rubisco's performance can enhance crop yield and stress tolerance (Von Caemmerer, 2020; Prywes et al, 2023). It has been documented that overexpression of Rubisco could increase photosynthesis capacity and growth advantage under chilling stress in maize (Salesse‐Smith et al, 2020), as well as grain yield and sustainability under heat stress in rice (Yoon et al, 2020), while knockdown of OsRBCS2 and OsRBCS4 caused significantly reduced yield (Maheshwari et al, 2021). We found that OsEIN2 and OsEIL1/2 inhibited expression of OsRBCS2/3/4 (Figure 5a), indicating that OsEIN2‐OsEIL1/2 pathway has negative impact on rice photosynthesis capacity and chilling tolerance.…”

Section: Discussionmentioning

confidence: 99%

OsEIN2‐OsEIL1/2 pathway negatively regulates chilling tolerance by attenuating OsICE1 function in rice

Zhai,

Chen,

Pan

et al. 2024

Plant Cell & Environment

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Low temperature severely affects rice development and yield. Ethylene signal is essential for plant development and stress response. Here, we reported that the OsEIN2‐OsEIL1/2 pathway reduced OsICE1‐dependent chilling tolerance in rice. The overexpressing plants of OsEIN2, OsEIL1 and OsEIL2 exhibited severe stress symptoms with excessive reactive oxygen species (ROS) accumulation under chilling, while the mutants (osein2 and oseil1) and OsEIL2‐RNA interference plants (OsEIL2‐Ri) showed the enhanced chilling tolerance. We validated that OsEIL1 and OsEIL2 could form a heterxodimer and synergistically repressed OsICE1 expression by binding to its promoter. The expression of OsICE1 target genes, ROS scavenging‐ and photosynthesis‐related genes were downregulated by OsEIN2 and OsEIL1/2, which were activated by OsICE1, suggesting that OsEIN2‐OsEIL1/2 pathway might mediate ROS accumulation and photosynthetic capacity under chilling by attenuating OsICE1 function. Moreover, the association analysis of the seedling chilling tolerance with the haplotype showed that the lower expression of OsEIL1 and OsEIL2 caused by natural variation might confer chilling tolerance on rice seedlings. Finally, we generated OsEIL2‐edited rice with an enhanced chilling tolerance. Taken together, our findings reveal a possible mechanism integrating OsEIN2‐OsEIL1/2 pathway with OsICE1‐dependent cascade in regulating chilling tolerance, providing a practical strategy for breeding chilling‐tolerant rice.

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Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells

Cited by 11 publications

References 32 publications

Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO₂assimilation in plants

OsEIN2‐OsEIL1/2 pathway negatively regulates chilling tolerance by attenuating OsICE1 function in rice

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Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells

Cited by 11 publications

References 32 publications

Rubisco is evolving for improved catalytic efficiency and CO 2 assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO 2 assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO2assimilation in plants

OsEIN2‐OsEIL1/2 pathway negatively regulates chilling tolerance by attenuating OsICE1 function in rice

Contact Info

Product

Resources

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Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO ₂ assimilation in plants

Rubisco is evolving for improved catalytic efficiency and CO₂assimilation in plants