Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco - Test2 - elhamkhani - TriplyDB

Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco

Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco

http://www.wikidata.org/entity/Q30160065

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Rubisco activity and regulation as targets for crop improvement Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco Structural mechanism of RuBisCO activation by carbamylation of the active site lysine Quantitative analysis of an engineered CO2-fixing Escherichia coli reveals great potential of heterotrophic CO2 fixation Molecular evolution of rbcL in three gymnosperm families: identifying adaptive and coevolutionary patterns Role of small subunit in mediating assembly of red-type form I Rubisco.Highly conserved small subunit residues influence rubisco large subunit catalysis.Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity.Engineering chloroplasts to improve Rubisco catalysis: prospects for translating improvements into food and fiber crops.Widespread positive selection in the photosynthetic Rubisco enzyme.Future CO2 concentrations, though not warmer temperatures, enhance wheat photosynthesis temperature responses.Development of an activity-directed selection system enabled significant improvement of the carboxylation efficiency of Rubisco Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in chlamydomonas.Cytonuclear evolution of rubisco in four allopolyploid lineages.Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.Isoleucine 309 acts as a C4 catalytic switch that increases ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) carboxylation rate in Flaveria A step forward to building an algal pyrenoid in higher plants.Rubisco catalytic properties of wild and domesticated relatives provide scope for improving wheat photosynthesis.Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research.A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.Stability-activity tradeoffs constrain the adaptive evolution of RubisCO.Can phenotypic plasticity in Rubisco performance contribute to photosynthetic acclimation?Temperature responses of the Rubisco maximum carboxylase activity across domains of life: phylogenetic signals, trade-offs, and importance for carbon gain.The CO2 concentrating mechanism and photosynthetic carbon assimilation in limiting CO2 : how Chlamydomonas works against the gradient.Synthetic CO2-fixation enzyme cascades immobilized on self-assembled nanostructures that enhance CO2/O2 selectivity of RubisCO Large-scale insertional mutagenesis of Chlamydomonas supports phylogenomic functional prediction of photosynthetic genes and analysis of classical acetate-requiring mutants.Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency.RubisCO selection using the vigorously aerobic and metabolically versatile bacterium Ralstonia eutropha.Engineering Rubisco activase from thermophilic cyanobacteria into high-temperature sensitive plants.Rubisco oligomers composed of linked small and large subunits assemble in tobacco plastids and have higher affinities for CO2 and O2.Surveying Rubisco Diversity and Temperature Response to Improve Crop Photosynthetic Efficiency.Temperature dependence of in vitro Rubisco kinetics in species of Flaveria with different photosynthetic mechanisms.Surveying the expanding prokaryotic Rubisco multiverse.Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphate.Substitutions at the opening of the Rubisco central solvent channel affect holoenzyme stability and CO2/O 2 specificity but not activation by Rubisco activase.The benefits of photorespiratory bypasses: how can they work?Positive Selection Driving Cytoplasmic Genome Evolution of the Medicinally Important Ginseng Plant Genus Panax.

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Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco

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Phylogenetic engineering at an ...... ic properties to algal Rubisco

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii

Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate

CO2 concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution

Substitutions at the Asp-473 latch residue of chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO(2)/O(2) specificity.

Assessment of structural and functional divergence far from the large subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase.

Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase.

Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase.

Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase.

Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase.

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