Relevant bibliographies by topics / Rubisco

Academic literature on the topic 'Rubisco'

Author: Grafiati

Published: 4 June 2021

Last updated: 22 June 2024

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Journal articles on the topic "Rubisco":

Valente, Ana I., Ana M. Ferreira, Mafalda R. Almeida, Aminou Mohamadou, Mara G. Freire, and Ana P. M. Tavares. "Efficient Extraction of the RuBisCO Enzyme from Spinach Leaves Using Aqueous Solutions of Biocompatible Ionic Liquids." Sustainable Chemistry 3, no. 1 (December 24, 2021): 1–18. http://dx.doi.org/10.3390/suschem3010001.

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Ribulose-1,5-biphosphate carboxylase/oxygenase (RuBisCO) is the most abundant protein on the planet, being present in plants, algae and various species of bacteria, with application in the pharmaceutical, chemical, cosmetic and food industries. However, current extraction methods of RuBisCO do not allow high yields of extraction. Therefore, the development of an efficient and selective RuBisCOs’ extraction method is required. In this work, aqueous solutions of biocompatible ionic liquids (ILs), i.e., ILs derived from choline and analogues of glycine-betaine, were applied in the RuBisCO’s extraction from spinach leaves. Three commercial imidazolium-based ILs were also investigated for comparison purposes. To optimize RuBisCO’s extraction conditions, response surface methodology was applied. Under optimum extraction conditions, extraction yields of 10.92 and 10.57 mg of RuBisCO/g of biomass were obtained with the ILs cholinium acetate ([Ch][Ac]) and cholinium chloride ([Ch]Cl), respectively. Circular dichroism (CD) spectroscopy results show that the secondary structure of RuBisCO is better preserved in the IL solutions when compared to the commonly used extraction solvent. The obtained results indicate that cholinium-based ILs are a promising and viable alternative for the extraction of RuBisCO from vegetable biomass.

McNevin, Dennis B., Murray R. Badger, Spencer M. Whitney, Susanne von Caemmerer, Guillaume G. B. Tcherkez, and Graham D. Farquhar. "Differences in Carbon Isotope Discrimination of Three Variants of D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Reflect Differences in Their Catalytic Mechanisms." Journal of Biological Chemistry 282, no. 49 (October 9, 2007): 36068–76. http://dx.doi.org/10.1074/jbc.m706274200.

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The carboxylation kinetic (stable carbon) isotope effect was measured for purified d-ribulose-1,5-bisphosphate carboxylases/oxygenases (Rubiscos) with aqueous CO2 as substrate by monitoring Rayleigh fractionation using membrane inlet mass spectrometry. This resulted in discriminations (Δ) of 27.4 ± 0.9‰ for wild-type tobacco Rubisco, 22.2 ± 2.1‰ for Rhodospirillum rubrum Rubisco, and 11.2 ± 1.6‰ for a large subunit mutant of tobacco Rubisco in which Leu335 is mutated to valine (L335V). These Δ values are consistent with the photosynthetic discrimination determined for wild-type tobacco and transplastomic tobacco lines that exclusively produce R. rubrum or L335V Rubisco. The Δ values are indicative of the potential evolutionary variability of Δ values for a range of Rubiscos from different species: Form I Rubisco from higher plants; prokaryotic Rubiscos, including Form II; and the L335V mutant. We explore the implications of these Δ values for the Rubisco catalytic mechanism and suggest that Rubiscos that are associated with a lower Δ value have a less product-like carboxylation transition state and/or allow a decarboxylation step that evolution has excluded in higher plants.

Whitney, Spencer M., and T. John Andrews. "The CO2/O2 specificity of single-subunit ribulose-bisphosphate carboxylase from the dinoflagellate, Amphidinium carterae." Functional Plant Biology 25, no. 2 (1998): 131. http://dx.doi.org/10.1071/pp97131.

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Some dinoflagellates have been shown recently to be unique among eukaryotes in having a ribulose-bisphosphate carboxylase-oxygenase (Rubisco, EC 4.1.1.39) composed of only one type of subunit, the 53-kDa large subunit [reviewed by Palmer, J.D. (1996) Plant Cell 8, 343–345]. Formerly, such homomeric Rubiscos had been found only in anaerobic bacteria and are characterised by such poor abilities to discriminate against the competitive alternate substrate, O2, that they would not be able to support net carbon gain if exposed to the current atmospheric CO2/O2 ratio. The capacity of Rubiscos from aerobic organisms to discriminate more effectively against O2 appeared to correlate with the presence of additional 12- to 18-kDa small subunits. Thus the CO2/O2 specificity of the homomeric dinoflagellate Rubisco is of considerable interest from the structural, physiological and evolutionary viewpoints. However, for unknown reasons, Rubiscos from dinoflagellates studied so far are so unstable after extraction from the cells that kinetic characterisation has not been possible. We redesigned two methods for measuring Rubisco’s CO2/O2 specificity to adapt them to rapid measurement at 10°C using unfractionated cell extracts. Both methods revealed that the CO2/O2 specificity of Rubisco from the dinoflagellate, Amphidinium carterae Hulburt, was approximately twice as great as that of other homomeric Rubiscos but unlikely to be sufficient to support dinoflagellate photosynthesis without assistance from an inorganic-carbon-concentrating mechanism.

Mueller-Cajar, Oliver, and Spencer M. Whitney. "Evolving improved Synechococcus Rubisco functional expression in Escherichia coli." Biochemical Journal 414, no. 2 (August 12, 2008): 205–14. http://dx.doi.org/10.1042/bj20080668.

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The photosynthetic CO2-fixing enzyme Rubisco [ribulose-P2 (D-ribulose-1,5-bisphosphate) carboxylase/oxygenase] has long been a target for engineering kinetic improvements. Towards this goal we used an RDE (Rubisco-dependent Escherichia coli) selection system to evolve Synechococcus PCC6301 Form I Rubisco under different selection pressures. In the fastest growing colonies, the Rubisco L (large) subunit substitutions I174V, Q212L, M262T, F345L or F345I were repeatedly selected and shown to increase functional Rubisco expression 4- to 7-fold in the RDE and 5- to 17-fold when expressed in XL1-Blue E. coli. Introducing the F345I L-subunit substitution into Synechococcus PCC7002 Rubisco improved its functional expression 11-fold in XL1-Blue cells but could not elicit functional Arabidopsis Rubisco expression in the bacterium. The L subunit substitutions L161M and M169L were complementary in improving Rubisco yield 11-fold, whereas individually they improved yield ∼5-fold. In XL1-Blue cells, additional GroE chaperonin enhanced expression of the I174V, Q212L and M262T mutant Rubiscos but engendered little change in the yield of the more assembly-competent F345I or F345L mutants. In contrast, the Rubisco chaperone RbcX stimulated functional assembly of wild-type and mutant Rubiscos. The kinetic properties of the mutated Rubiscos varied with noticeable reductions in carboxylation and oxygenation efficiency accompanying the Q212L mutation and a 2-fold increase in Kribulose-P2 (KM for the substrate ribulose-P2) for the F345L mutant, which was contrary to the ∼30% reductions in Kribulose-P2 for the other mutants. These results confirm the RDE systems versatility for identifying mutations that improve functional Rubisco expression in E. coli and provide an impetus for developing the system to screen for kinetic improvements.

Iqbal, Wasim A., Isabel G. Miller, Rebecca L. Moore, Iain J. Hope, Daniel Cowan-Turner, and Maxim V. Kapralov. "Rubisco substitutions predicted to enhance crop performance through carbon uptake modelling." Journal of Experimental Botany 72, no. 17 (June 11, 2021): 6066–75. http://dx.doi.org/10.1093/jxb/erab278.

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Abstract Improving the performance of the CO2-fixing enzyme Rubisco is among the targets for increasing crop yields. Here, Earth system model (ESM) representations of canopy C3 and C4 photosynthesis were combined with species-specific Rubisco parameters to quantify the consequences of bioengineering foreign Rubiscos into C3 and C4 crops under field conditions. The ‘two big leaf’ (sunlit/shaded) model for canopy photosynthesis was used together with species-specific Rubisco kinetic parameters including maximum rate (Kcat), Michaelis–Menten constant for CO2 at ambient atmospheric O2 (Kc21%O2), specificity for CO2 to O2 (Sc/o), and associated heat activation (Ha) values. Canopy-scale consequences of replacing native Rubiscos in wheat, maize, and sugar beet with foreign enzymes from 27 species were modelled using data from Ameriflux and Fluxnet databases. Variation among the included Rubisco kinetics differentially affected modelled carbon uptake rates, and Rubiscos from several species of C4 grasses showed the greatest potential of >50% carbon uptake improvement in wheat, and >25% improvement in sugar beet and maize. This study also reaffirms the need for data on fully characterized Rubiscos from more species, and for better parameterization of ‘Vcmax’ and temperature response of ‘Jmax’ in ESMs.

Utåker, Janne B., Kjell Andersen, Ågot Aakra, Birgitte Moen, and Ingolf F. Nes. "Phylogeny and Functional Expression of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from the Autotrophic Ammonia-Oxidizing Bacterium Nitrosospira sp.Isolate 40KI." Journal of Bacteriology 184, no. 2 (January 15, 2002): 468–78. http://dx.doi.org/10.1128/jb.184.2.468-478.2002.

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ABSTRACT The autotrophic ammonia-oxidizing bacteria (AOB), which play an important role in the global nitrogen cycle, assimilate CO2 by using ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). Here we describe the first detailed study of RubisCO (cbb) genes and proteins from the AOB. The cbbLS genes from Nitrosospira sp. isolate 40KI were cloned and sequenced. Partial sequences of the RubisCO large subunit (CbbL) from 13 other AOB belonging to the β and γ subgroups of the class Proteobacteria are also presented. All except one of the β-subgroup AOB possessed a red-like type I RubisCO with high sequence similarity to the Ralstonia eutropha enzyme. All of these new red-like RubisCOs had a unique six-amino-acid insert in CbbL. Two of the AOB, Nitrosococcus halophilus Nc4 and Nitrosomonas europaea Nm50, had a green-like RubisCO. With one exception, the phylogeny of the AOB CbbL was very similar to that of the 16S rRNA gene. The presence of a green-like RubisCO in N. europaea was surprising, as all of the other β-subgroup AOB had red-like RubisCOs. The green-like enzyme of N. europaea Nm50 was probably acquired by horizontal gene transfer. Functional expression of Nitrosospira sp. isolate 40KI RubisCO in the chemoautotrophic host R. eutropha was demonstrated. Use of an expression vector harboring the R. eutropha cbb control region allowed regulated expression of Nitrosospira sp. isolate 40KI RubisCO in an R. eutropha cbb deletion strain. The Nitrosospira RubisCO supported autotrophic growth of R. eutropha with a doubling time of 4.6 h. This expression system may allow further functional analysis of AOB cbb genes.

Ng, Jediael, Zhijun Guo, and Oliver Mueller-Cajar. "Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco." Journal of Biological Chemistry 295, no. 48 (September 18, 2020): 16427–35. http://dx.doi.org/10.1074/jbc.ra120.015759.

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The photosynthetic CO2 fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) forms dead-end inhibited complexes while binding multiple sugar phosphates, including its substrate ribulose 1,5-bisphosphate. Rubisco can be rescued from this inhibited form by molecular chaperones belonging to the ATPases associated with diverse cellular activities (AAA+ proteins) termed Rubisco activases (Rcas). The mechanism of green-type Rca found in higher plants has proved elusive, in part because until recently higher-plant Rubiscos could not be expressed recombinantly. Identifying the interaction sites between Rubisco and Rca is critical to formulate mechanistic hypotheses. Toward that end here we purify and characterize a suite of 33 Arabidopsis Rubisco mutants for their ability to be activated by Rca. Mutation of 17 surface-exposed large subunit residues did not yield variants that were perturbed in their interaction with Rca. In contrast, we find that Rca activity is highly sensitive to truncations and mutations in the conserved N terminus of the Rubisco large subunit. Large subunits lacking residues 1–4 are functional Rubiscos but cannot be activated. Both T5A and T7A substitutions result in functional carboxylases that are poorly activated by Rca, indicating the side chains of these residues form a critical interaction with the chaperone. Many other AAA+ proteins function by threading macromolecules through a central pore of a disc-shaped hexamer. Our results are consistent with a model in which Rca transiently threads the Rubisco large subunit N terminus through the axial pore of the AAA+ hexamer.

Wang, Renée Z., Albert K. Liu, Douglas M. Banda, Woodward W. Fischer, and Patrick M. Shih. "A Bacterial Form I’ Rubisco Has a Smaller Carbon Isotope Fractionation than Its Form I Counterpart." Biomolecules 13, no. 4 (March 26, 2023): 596. http://dx.doi.org/10.3390/biom13040596.

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Form I rubiscos evolved in Cyanobacteria ≥ 2.5 billion years ago and are enzymatically unique due to the presence of small subunits (RbcS) capping both ends of an octameric large subunit (RbcL) rubisco assembly to form a hexadecameric (L8S8) holoenzyme. Although RbcS was previously thought to be integral to Form I rubisco stability, the recent discovery of a closely related sister clade of octameric rubiscos (Form I’; L8) demonstrates that the L8 complex can assemble without small subunits (Banda et al. 2020). Rubisco also displays a kinetic isotope effect (KIE) where the 3PG product is depleted in 13C relative to 12C. In Cyanobacteria, only two Form I KIE measurements exist, making interpretation of bacterial carbon isotope data difficult. To aid comparison, we measured in vitro the KIEs of Form I’ (Candidatus Promineofilum breve) and Form I (Synechococcus elongatus PCC 6301) rubiscos and found the KIE to be smaller in the L8 rubisco (16.25 ± 1.36‰ vs. 22.42 ± 2.37‰, respectively). Therefore, while small subunits may not be necessary for protein stability, they may affect the KIE. Our findings may provide insight into the function of RbcS and allow more refined interpretation of environmental carbon isotope data.

Loganathan, Nitin, Yi-Chin Candace Tsai, and Oliver Mueller-Cajar. "Characterization of the heterooligomeric red-type rubisco activase from red algae." Proceedings of the National Academy of Sciences 113, no. 49 (November 21, 2016): 14019–24. http://dx.doi.org/10.1073/pnas.1610758113.

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The photosynthetic CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) is inhibited by nonproductive binding of its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. Reactivation requires ATP-hydrolysis–powered remodeling of the inhibited complexes by diverse molecular chaperones known as rubisco activases (Rcas). Eukaryotic phytoplankton of the red plastid lineage contain so-called red-type rubiscos, some of which have been shown to possess superior kinetic properties to green-type rubiscos found in higher plants. These organisms are known to encode multiple homologs of CbbX, the α-proteobacterial red-type activase. Here we show that the gene products of two cbbX genes encoded by the nuclear and plastid genomes of the red algae Cyanidioschyzon merolae are nonfunctional in isolation, but together form a thermostable heterooligomeric Rca that can use both α-proteobacterial and red algal-inhibited rubisco complexes as a substrate. The mechanism of rubisco activation appears conserved between the bacterial and the algal systems and involves threading of the rubisco large subunit C terminus. Whereas binding of the allosteric regulator RuBP induces oligomeric transitions to the bacterial activase, it merely enhances the kinetics of ATP hydrolysis in the algal enzyme. Mutational analysis of nuclear and plastid isoforms demonstrates strong coordination between the subunits and implicates the nuclear-encoded subunit as being functionally dominant. The plastid-encoded subunit may be catalytically inert. Efforts to enhance crop photosynthesis by transplanting red algal rubiscos with enhanced kinetics will need to take into account the requirement for a compatible Rca.

Tabita, F. Robert, Thomas E. Hanson, Huiying Li, Sriram Satagopan, Jaya Singh, and Sum Chan. "Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs." Microbiology and Molecular Biology Reviews 71, no. 4 (December 2007): 576–99. http://dx.doi.org/10.1128/mmbr.00015-07.

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SUMMARY About 30 years have now passed since it was discovered that microbes synthesize RubisCO molecules that differ from the typical plant paradigm. RubisCOs of forms I, II, and III catalyze CO2 fixation reactions, albeit for potentially different physiological purposes, while the RubisCO-like protein (RLP) (form IV RubisCO) has evolved, thus far at least, to catalyze reactions that are important for sulfur metabolism. RubisCO is the major global CO2 fixation catalyst, and RLP is a somewhat related protein, exemplified by the fact that some of the latter proteins, along with RubisCO, catalyze similar enolization reactions as a part of their respective catalytic mechanisms. RLP in some organisms catalyzes a key reaction of a methionine salvage pathway, while in green sulfur bacteria, RLP plays a role in oxidative thiosulfate metabolism. In many organisms, the function of RLP is unknown. Indeed, there now appear to be at least six different clades of RLP molecules found in nature. Consideration of the many RubisCO (forms I, II, and III) and RLP (form IV) sequences in the database has subsequently led to a coherent picture of how these proteins may have evolved, with a form III RubisCO arising from the Methanomicrobia as the most likely ultimate source of all RubisCO and RLP lineages. In addition, structure-function analyses of RLP and RubisCO have provided information as to how the active sites of these proteins have evolved for their specific functions.

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Dissertations / Theses on the topic "Rubisco":

Milward, Sara Eve. "Interrogating plant Rubisco-Rubisco activase interactions." Phd thesis, Canberra, ACT : The Australian National University, 2018. http://hdl.handle.net/1885/149565.

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Atmospheric CO2 fixation is catalysed by the photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Despite the critical role Rubisco plays in the biosphere, it is a slow catalyst that poorly discriminates between substrate CO2 and O2, and is often the rate-limiting step of photosynthesis. These deficiencies have made improving Rubisco function a major target in steps towards enhancing leaf photosynthesis rate and plant growth. In pursuing this goal, one strategy is to identify solutions for improving the kinetics of plant Rubisco and introduce these altered Rubisco isoforms into crops (Sharwood, 2017). Unfortunately efforts to improve the performance of plant Rubiscos have so far proven unsuccessful. Success appears to be hindered by Rubisco’s complex catalytic mechanism and the extensive array of accessory proteins needed to assemble the eight large (L) and eight small (S) subunits into a L8S8 complex and to maintain it in a functional form. The complex catalytic chemistry of Rubisco is prone to inhibition by various sugar-phosphate ligands. These include catalytic misfire products as well as its own substrate, ribulose-1,5-bisphosphate (RuBP), which forms an inactive Rubisco-RuBP (ER) complex when bound to non-carbamylated (i.e. non-activated) catalytic sites. Release of these inhibitors is mediated by the AAA+ (ATPases associated with a variety of cellular activities) protein Rubisco activase (Rca); a Rubisco-specific metabolic repair chaperone for which there are convergently evolved structural isoforms found in most photosynthetic organisms (Bhat et al., 2017a; Mueller-Cajar, 2017). Rca is now also a promising target for manipulating photosynthetic performance, especially under elevated temperature stress and fluctuating light (Carmo-Silva & Salvucci, 2013; Kumar et al., 2009; Kurek et al., 2007; Scafaro et al., 2016; Yamori et al., 2012). Critical to future Rubisco and Rca engineering efforts in plants is a greater mechanistic understanding of how Rca interacts with Rubisco, and the extent to which the kinetics of Rca differ between plant species. Utilising chloroplast transformation in tobacco, this thesis investigated the H9 helix and N-terminal region of Rca, and the βC-βD loop and C terminus of the Rubisco large (L-) subunit (RbcL) to determine their role in the Rubisco-Rca interaction in plants using both in vivo and in vitro methods. Capitalising on the regulatory incompatibility between Rubisco and Rca enzymes from Solanaceae and non-Solanaceae species, this thesis examined how mutations in the tobacco (Solanaceae) and Flaveria (F. bidentis and F. floridana, non-Solanaceae) enzymes influenced their kinetic properties and the Rca activation potential for inhibited ER complexes. The ability to continuously monitor the rate of ER activation provided by a NADH-coupled spectrophotometric method made it preferential to the alternative two-step 14CO2-fixation assay method. Optimising the assay conditions, particularly the accurate determination of enzyme concentrations, was crucial for obtaining reproducible kinetic values. Normalising the measurements of ER activation rate relative to the Rca ATPase activity (kcatATP ) proved critical in providing a means to determine the effect the Rca and Rubisco mutations had on interactivity. Using these assay conditions, mutagenic analyses of the Rca H9 helix found residue 317 plays a dominant role in defining the Rubisco selectivity of NtRca, and is critical for functional FbRca. N-terminal domain swapping modifications to NtRca and FbRca revealed amino acids at the junction of the N-terminal extension and the AAA+ module (residues 50 to 85) significantly influenced both kcatATP and the potential to interact with their cognate Rubiscos, but had little influence on altering interaction with the non-native Rubisco. In vivo analysis of Rubisco-Rca interaction was undertaken using tobacco genotypes producing differing tobacco Rubisco or recombinant Flaveria Rubisco mutants generated by chloroplast transformation of the rbcL gene into the plastome. In vitro analysis using purified enzymes uniformly showed residues 89 and 94 of the βC-βD loop of the F. bidentis, F. floridana and tobacco RbcLs influence interaction with Rca. In contrast, in vivo leaf gas exchange measurements of photosynthetic induction in the tobacco genotypes producing mutant RbcL showed mutation of residues 89 and 94 had little to no influence on their capacity to be activated by the endogenous NtRca. Combinatorial in vitro analyses using the range of RbcL and Rca mutants generated in this study were undertaken to better understand their interaction mechanism. It was found the avidity of Rubisco-Rca interactions were primarily defined by residue 94 in RbcL and 317 in Rca, and less so by RbcL residue 89 and Rca residue 320. Mutations to the RbcL C terminus had little influence on plant Rubisco-Rca interactions except when coupled with mutations that disrupted the connection between the RbcL βC-βD loop and the Rca H9 helix. The cumulative effect of the RbcL βC-βD loop and C-terminal modifications on Rubisco-Rca interactivity of these mutants implies involvement of the RbcL C terminus in the activation mechanism of Rca. This thesis showcases a novel approach to study the mechanism of plant Rubisco-Rca interactions by generating mutant Rubisco variants through tobacco plastome transformation. The work highlights large variations in the kinetics of NtRca (Solanaceae) and FbRca (non-Solanaceae) and provides evidence for variations in their Rubisco activation mechanism. For instance, while a D317K substitution in NtRca significantly enhanced its ability to activate Flaveria Rubisco, the reciprocal K317D mutation in FbRca had little impact on improving its capacity to activate tobacco Rubisco. Improving our understanding of the mechanistic differences in plant Rubisco-Rca interactions is critical for future Rubisco engineering endeavours. It is especially relevant in the context of ongoing efforts to transplant more efficient Rubisco variants into leaf chloroplasts where co-transformation with an appropriate Rca may be needed. Potential transgenic strategies for co-engineering compatible Rubisco and Rca isoforms in planta are also discussed.

Keown, Jeremy Russell. "Rubisco's chiropractor: a study of higher plant Rubisco activase." Thesis, University of Canterbury. School of Biology, 2015. http://hdl.handle.net/10092/10398.

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Rubisco activase operates as the chaperone responsible for maintaining the catalytic competency of Ribulose 1,5-bisphophate carboxylase oxygenase (Rubisco) in plants. Rubisco is notoriously inefficient, rapidly self-inactivating under physiological conditions. Rubisco activase uses the power released from the hydrolysis of ATP to power a conformational change in Rubisco, reactivating it. Rubisco activase has been previously shown to form a large range of species in solution; however, little has been done to relate the size of oligomeric species and physiological activity. In this thesis data is presented from a range of biophysical techniques including analytical ultracentrifugation, static light scattering, and small angle X-ray scattering combined with activity assays to show a strong relationship between oligomeric state and activity. The results suggest that small oligomers comprising 2-4 subunits are sufficient to attain full specific activity, a highly unusual property for enzymes from the AAA+ family. Studies utilising a number of Rubisco activase variants enabled the determination of how Rubisco and Rubisco activase may interact within a plant cell. A detailed characterisation of the α-, β-, and a mixture of isoforms further broadened our knowledge on the oligomerisation of Rubisco activase. Of particular importance was the discovery of a thermally stable hexameric Rubisco activase variant. It is hoped that these findings may contribute to development of more heat tolerant Rubisco activase and lead research into more drought resilient crop plants.

Saschenbrecker, Sandra. "Folding and assembly of RuBisCO." Diss., lmu, 2007. http://nbn-resolving.de/urn:nbn:de:bvb:19-75775.

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Girnus, Jan. "Regulation of Rubisco in CAM plants." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.616010.

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Singh, Jaya. "Functional Relationships Among Rubisco Family Members." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1220413240.

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Bošková, Martina. "Vliv stáří jehlic na obsah a aktivitu enzymu Rubisco u smrku ztepilého v podmínkách normální a zvýšené koncentrace CO2." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2009. http://www.nusl.cz/ntk/nusl-216513.

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In this diploma work influence of needle age at Rubisco activity and content in Norway spruce (Picea abies) was studied. The plants were cultivated in conditions with ambient (A) CO2 concentration (350 µmol CO2/mol) and elevated (E) CO2 concentration (700 µmol CO2/mol). Sampling was done two times during the growing season (in the middle of June and in the end of September) were taken. Initial and total Rubisco activities were measured spectrophotometrically. Rubisco content was determined by SDS–PAGE method. Rubisco activity in 18-months-old needles was in E higher than in A. Rubisco contents in current-year needles and one-year-old needles were in A higher than in E in September. These differences were statistically significant that demonstrates the down-regulation of Rubisco content in conditions of elevated CO2 concentration. It seems the course of activities and content depending on age of the needles are antiparallel, that means that decrease of content is followed by increase of activity.

Butt, Mohammed Salman. "Technologies and methods to characterise Rubisco function." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/39375.

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Almost every carbon atom that our bodies are made of and clothed in, at one point or another saw the active site of the enzyme, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). This enzyme, one of the largest in nature at ~550 kDa, is also said to be the most abundant in nature, constituting up to 50% of soluble protein in land plants. It is however, notoriously inefficient at fixing carbon dioxide, due to its slow catalytic turnover, low affinity for atmospheric CO2, and its use of both CO2 and O2 as substrates for competing reactions. For this reason, Rubisco has also been one of the most intensively studied enzymes. The potential harvest yield of crops has been shown to be limited by the rate at which atmospheric carbon is fixed by Rubisco. As a result much focus is on studying and engineering Rubisco in order to increase the overall efficiency of biomass production, to cope with the fuel, fibre and food needs of a growing global population. Since Rubisco is one component of a system, the demand for developing tools to study and engineer Rubisco in light of its wider interactome and regulatory networks, is ever increasing. This thesis describes the development of tools to study the function of Rubisco. It includes the development of a novel method for purifying the enzyme using hydrophobic interaction chromatography. Different populations of Rubisco were isolated with distinct maximal rates of carboxylation, possibly reflecting differences in hydrophobic characteristics. It also contains the development of a spectroscopic activity assay for Rubisco activity, and an enzyme-linked immunosorbent assay (ELISA) for Rubisco and its catalytic chaperone, Rubisco Activase. These tools were then applied to investigate the influence of cellulose biosynthesis inhibition (CBI) on Rubisco in Arabidopsis seedlings, to investigate any potential sink-regulation of the activity or levels of Rubisco. It was found that specific Rubisco activity was reduced as a result of CBI, and rescued by providing osmotic support, thus implicating turgor pressure as a potential mechanism. Finally, preliminary results were obtained which demonstrate the potential of mass spectrometry for measuring relative levels of Rubisco ions generated by MALDI (matrix-assisted laser desorption ionisation), showing that this can be a useful method for use in interactome studies in conjunction with other tools.

Wietrzynski, Wojciech. "Rubisco biogenesis and assembly in Chlamydomonas reinhardtii." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066336/document.

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La nécessité de coordonner l’expression des gènes provenant de génomes différents chez les plantes a conduit à l’émergence de mécanismes imposant un contrôle nucléaire sur l’expression génétique de l’organelle. Des signaux antérogrades, exercés par des protéines reconnaissant des séquences spécifiques, existent en parallèle avec un contrôle des synthèses chloroplastiques dépendant de l’assemblage (CES). Ensemble, ils coordonnent la formation stoichiométrique des complexes photosynthétiques.La Ribulose bisphosphate carboxylase/oxygénase (Rubisco) est une enzyme localisée dans le chloroplaste qui contient deux sous-unités. La grande sous-unité (LSU) et la petite sous-unité (SSU) sont codées par les génomes chloroplastique et nucléaire respectivement. Elles s’assemblent dans le stroma du chloroplaste pour former une holoenzyme hexadécamérique (LSU8SSU8). Pendant mon travail au laboratoire, j’ai tenté de décrire les étapes régulatrices majeures de la synthèse de la Rubisco chez Chlamydomonas reinhardtii en me focalisant sur la régulation post-transcriptionelle de la LSU.J’ai montré que la protéine PPR – MRL1 est un facteur limitant pour l’accumulation de l’ARN messager de rbcL. Bien qu’il ait été décrit précédemment comme un facteur stabilisateur du transcrit susnommé, MRL1 s’est révélé avoir un rôle dans la traduction.J’ai par ailleurs démontré que chez Chlamydomonas, l’expression de la Rubisco est contrôlée par la présence de la SSU. En son absence, la traduction de rbcL est inhibée par son propre produit – la grande sous-unité non assemblée. J’ai pu montrer qu’un intermédiaire d’assemblage, constitué de LSU en complexe avec sa chaperonne RAF1, est nécessaire pour cette régulation, ce qui prouve que ce processus dépend de l’état d’oligomérisation de la LSU. Parallèlement, j’ai caractérisé le devenir de la LSU non assemblée quand la régulation CES est perturbée, et grâce à cela ait contribué à améliorer la connaissance de son processus de repliement et d’assemblage
The necessity to coordinate the expression of genes originating from different genomes within the plant cell resulted in the appearance of mechanisms imposing nuclear control over organelle gene expression. Anterograde signaling through sequence-specific trans-acting proteins (OTAFs) coexists in the chloroplast with an assembly dependent control of chloroplast synthesis (CES process) that coordinates the stoichiometric formation of photosynthetic complexes.Ribulose bisphosphate carboxylase/oxygenase (Rubisco) is a chloroplast-located carbon fixing enzyme constituted of two subunits. Large subunit (LSU) and small subunit (SSU) are encoded in the chloroplast and nuclear genomes respectively. In the stroma they assemble to form a hexadecameric holoenzyme (LSU8SSU8). In this study I tried to highlight major regulatory points of its synthesis in Chlamydomonas reinhardtii focusing on the posttranscriptional regulation of LSU.I showed that the MRL1 PPR protein is a limiting factor for rbcL mRNA accumulation. Whereas it has been previously designated as a stabilization factor for the abovementioned transcript, MRL1 appeared also to have a function in rbcL translation.Most notably, I have demonstrated that in Chlamydomonas reinhardtii Rubisco expression is controlled by the small subunit (SSU) presence. In its absence rbcL undergoes an inhibition of translation through its own product – the unassembled Rubisco large subunit. This process depends on LSU-oligomerization state as I was able to show that the presence of a high order LSU assembly intermediate bound to the RAF1 assembly chaperone is essential for the regulation to occur. In parallel I shed light on the fate of unassembled LSU in a deregulated CES context, thereby improving our understanding of the process of its folding and assembly

Wietrzynski, Wojciech. "Rubisco biogenesis and assembly in Chlamydomonas reinhardtii." Electronic Thesis or Diss., Paris 6, 2017. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2017PA066336.pdf.

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Zítková, Jana. "Vliv zvýšené koncentrace oxidu uhličitého na denní chod obsahu a aktivity enzymu Rubisco." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2011. http://www.nusl.cz/ntk/nusl-216688.

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Diurnal changes of initial and total activity and content of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) under conditions of ambient (350 µmol mol-1) and elevated (E = 700 µmol mol 1) concentration CO2 were measured in needles of Norway spruce. Needles of Norway spruce were taken on 22th July in two-hours from 3:30 a. m. till 10:30 p. m. The Rubisco activity was determined by spectrophotometry, the Rubisco content was detected by SDS-PAGE. The Rubisco activity was in most samples statistically significantly lower in needles cutlivated under ambient carbon dioxide then in needles cultivated under elevated carbon dioxide. Diagrams of the Rubisco activity shows absence of night inhibitor CA1P. The Rubisco activity was directly proportional to the intensity of photosynthetically active radiation in time from 7:00 a. m. till 7:30 p. m. The Rubisco content was statistically significantly higher in needles of Norway spruce cultivated under ambient carbon dioxide than in needles cultivated under elevated CO2, which shows acclimation of the Rubisco content during long-term effect of elevated CO2 concentration.

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Books on the topic "Rubisco":

Martin, Gillian Clare. The use of Rubisco in the study of orchid hybridization. Birmingham: Universityof Birmingham, 1987.

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Galmés, Jeroni. La Rubisco, el punt d'inici de la vida: Significat ecològic i una possible clau per a la millora genètica de la productivitat vegetal. Palma: Hiperdimensional, 2006.

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Kopf, Gail. Rubicon. Nashville: T. Nelson Publishers, 1993.

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John, Hooker. Rubicon. Ringwood, Vic., Australia: Penguin Books, 1991.

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Alexander, Lawrence. Rubicon. New York: William Morrow, 2008.

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Saylor, Steven. Rubicon. New York: St. Martin's Press, 1999.

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Garamvölgyi, László. Rubicon. Budapest: BTR Kft., 2000.

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Erickson, Steve. Rubicon Beach. New York: Vintage Books, 1987.

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Dennis, Jones. Rubicon one. London: Arrow, 1985.

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Erickson, Steve. Rubicon Beach. New York: Poseidon Press, 1986.

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Book chapters on the topic "Rubisco":

Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 1485. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1395.

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Liu, Cuimin, Kaiyao Huang, and Jianrong Xia. "Rubisco." In Research Methods of Environmental Physiology in Aquatic Sciences, 65–74. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-5354-7_7.

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Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 2224. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1395.

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Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1395-2.

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Peretó, Juli. "Rubisco." In Encyclopedia of Astrobiology, 2702. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1395.

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Andrews, T. John, Susanne von Caemmerer, Colleen J. Mate, Graham S. Hudson, and John R. Evans. "The Regulation of Rubisco Catalysis by Rubisco Activase." In Photosynthesis: from Light to Biosphere, 3909–14. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_920.

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Portis, Archie R., Brian Esau, Eric M. Larson, Genhai Zhu, Chris J. Chastain, Carolyn M. O’Brien, and Robert J. Spreitzer. "Characteristics of the Interaction between Rubisco and Rubisco Activase." In Photosynthesis: from Light to Biosphere, 3933–38. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_924.

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Haslam, Richard P., Alfred J. Keys, P. John Andralojc, Pippa J. Madgwick, Andersson Inger, Anette Grimsrud, Hans C. Eilertsen, and Martin A. J. Parry. "Specificity of diatom Rubisco." In Plant Responses to Air Pollution and Global Change, 157–64. Tokyo: Springer Japan, 2005. http://dx.doi.org/10.1007/4-431-31014-2_18.

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Andrews, T. John, Murray R. Badger, Daryl L. Edmondson, Heather J. Kane, Matthew K. Morell, and Kalanethee Paul. "Rubisco: Subunits and Mechanism." In Current Research in Photosynthesis, 2237–44. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_511.

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Wu, Xiang-yu, Wei Gu, and Guang-yao Wu. "Rubisco from Amaranthus Hypochondriacus." In Current Research in Photosynthesis, 2245–48. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_512.

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Conference papers on the topic "Rubisco":

Zhou, Hualu, Giang Vu, and David J. McClements. "Rubisco Proteins as Plant-based Alternatives to Egg White Proteins: Characterization of Thermal Gelation Properties." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/vamx3998.

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RuBisCO proteins can be isolated from abundant and sustainable plant sources, such as duckweed (e.g., Lemnoideae). These plant-based globular proteins are capable of irreversibly unfolding and forming gels when heated, which means they may be able to mimic some of the functional attributes exhibited by animal globular proteins. In this study, we examined the ability of RuBisCo proteins to mimic the initial rheology and thermal gelation properties of egg white, which the aim of developing plant-based egg analogs. The impact of protein concentration (10-15% w/w), pH (7 to 9), and calcium concentration (0 to 50 mM CaCl2) on the properties of the egg white analogs was examined. The appearance (colorimetry), thermal denaturation (differential scanning calorimetry), thermal gelation (dynamic shear rheology), and texture profiles (compression testing) were measured. RuBisCO-based egg white analogs could be successfully produced at 10% protein content and pH 8 in the absence of salt. These RuBisCO protein solutions had similar apparent viscosity-shear rate profiles, shear modulus-temperature profiles, gelling temperatures, and final gel strengths as egg white. However, there were some differences. RuBisCO protein gels were slightly darker than egg white, which was attributed to the presence of some phenolic impurities. RuBisCo protein exhibited a single thermal transition temperature (~ 66 ℃) whereas egg white exhibited two (~66 and ~81 ℃). RuBisCo protein gels were more brittle but less chewy and resilient than egg white gels. This study provides valuable insights into the potential of RuBisCo protein for formulating plant-based egg white analogs, which may help improve the sustainability of the modern food supply.

Callaghan, Jake. "NOVEL ARCHAEAL LINEAGES UTILIZING RUBISCO IN LAKE SUPERIOR SEDIMENTS." In 54th Annual GSA North-Central Section Meeting - 2020. Geological Society of America, 2020. http://dx.doi.org/10.1130/abs/2020nc-348067.

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Gao, Lan. "Structure of a Novel Rubisco Activase in Gardenia jasminoides." In 2018 2nd International Conference on Advances in Energy, Environment and Chemical Science (AEECS 2018). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/aeecs-18.2018.8.

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Kacar, Betul, Zachary R. Adam, Victor Hanson-Smith, and Nicholas Boekelheide. "CONSTRAINING THE GREAT OXIDATION EVENT WITHIN THE RUBISCO PHYLOGENETIC TREE." In GSA Annual Meeting in Denver, Colorado, USA - 2016. Geological Society of America, 2016. http://dx.doi.org/10.1130/abs/2016am-287360.

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Holden, Todd, S. Dehipawala, E. Cheung, R. Bienaime, J. Ye, G. Tremberger, Jr., P. Schneider, D. Lieberman, and T. Cheung. "Diverse nucleotide compositions and sequence fluctuation in Rubisco protein genes." In SPIE Optical Engineering + Applications, edited by Richard B. Hoover, Paul C. W. Davies, Gilbert V. Levin, and Alexei Y. Rozanov. SPIE, 2011. http://dx.doi.org/10.1117/12.893434.

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Babani, Salma I., Chukwuma C. Ogbaga, Dominic Okolo, and George Mangse. "Bioactive Compound and Rubisco Analyses of Leaf and Seed Extracts of Sesamum indicum." In 2019 15th International Conference on Electronics, Computer and Computation (ICECCO). IEEE, 2019. http://dx.doi.org/10.1109/icecco48375.2019.9043249.

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Yesiltas, Betül, Pedro J. García-Moreno, Egon B. Hansen, Paolo Marcatili, Tobias H. Olsen, Simon Gregersen, and Charlotte Jacobsen. "Antioxidant Activity of Peptides Embedded in Potato, Seaweed, Rubisco and Single Cell Proteins." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists’ Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.25.

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Subramani, Boopathi, and Kuo-Yuan Hwa. "In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family." In 2010 2nd International Conference on Information Technology Convergence and Services (ITCS). IEEE, 2010. http://dx.doi.org/10.1109/itcs.2010.5581267.

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Ogbaga, Chukwuma C., Rashida A. Maishanu, and Dominic Okolo. "Characterisation of the Rubisco Content and Bioactive Compound Analysis of Leaf and Seed Extracts of Tamarindus indica." In 2019 15th International Conference on Electronics, Computer and Computation (ICECCO). IEEE, 2019. http://dx.doi.org/10.1109/icecco48375.2019.9043238.

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Biswas, Ishita, and Debanjan Mitra. "Comparative Analysis of RuBisCO Evolution and Intrinsic Differences: Insights from In Silico Assessment in Cyanobacteria, Monocot, and Dicot Plants." In The 3rd International Electronic Conference on Agronomy. Basel Switzerland: MDPI, 2024. http://dx.doi.org/10.3390/iecag2023-15820.

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Reports on the topic "Rubisco":

Salvucci, Michael. Consequences of altering rubisco regulation. Office of Scientific and Technical Information (OSTI), December 2013. http://dx.doi.org/10.2172/1164812.

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Spreitzer, Robert Joseph. Role of the Rubisco Small Subunit. Office of Scientific and Technical Information (OSTI), November 2016. http://dx.doi.org/10.2172/1330984.

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Zielinski, R. (Structure and expression of nuclear genes encoding rubisco activase). Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/6993018.

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Hartman, F. C. Rubisco Mechanism: Dissection of the Enolization Partial Reaction. Final Report. Office of Scientific and Technical Information (OSTI), June 2003. http://dx.doi.org/10.2172/824531.

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Zielinski, R. E. Structure and expression of nuclear genes encoding rubisco activase. Final technical report. Office of Scientific and Technical Information (OSTI), June 1994. http://dx.doi.org/10.2172/10154999.

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Spreitzer, Robert J. Role of the Rubisco small subunit. Final report for period May 1, 1997--April 30,2000. Office of Scientific and Technical Information (OSTI), October 2000. http://dx.doi.org/10.2172/809467.

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Azem, Abdussalam, George Lorimer, and Adina Breiman. Molecular and in vivo Functions of the Chloroplast Chaperonins. United States Department of Agriculture, June 2011. http://dx.doi.org/10.32747/2011.7697111.bard.

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We present here the final report for our research project entitled "The molecular and in vivo functions of the chloroplast chaperonins”. Over the past few decades, intensive investigation of the bacterial GroELS system has led to a basic understanding of how chaperonins refold denatured proteins. However, the parallel is limited in its relevance to plant chaperonins, since the plant system differs from GroEL in genetic complexity, physiological roles of the chaperonins and precise molecular structure. Due to the importance of plant chaperonins for chloroplast biogenesis and Rubisco assembly, research on this topic will have implications for many vital applicative fields such as crop hardiness and efficiency of plant growth as well as the production of alternative energy sources. In this study, we set out to investigate the structure and function of chloroplast chaperonins from A. thaliana. Most plants harbor multiple genes for chaperonin proteins, making analysis of plant chaperonin systems more complicated than the GroEL-GroES system. We decided to focus on the chaperonins from A. thaliana since the genome of this plant has been well defined and many materials are available which can help facilitate studies using this system. Our proposal put forward a number of goals including cloning, purification, and characterization of the chloroplast cpn60 subunits, antibody preparation, gene expression patterns, in vivo analysis of oligomer composition, preparation and characterization of plant deletion mutants, identification of substrate proteins and biophysical studies. In this report, we describe the progress we have made in understanding the structure and function of chloroplast chaperonins in each of these categories.

Miller, John. Japan Crosses the Rubicon? Fort Belvoir, VA: Defense Technical Information Center, January 2002. http://dx.doi.org/10.21236/ada417346.

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Rubiano, Kristian, and Dalia C. Barragán Barrera. ¿Las áreas protegidas sí están protegiendo nuestra biodiversidad? Universidad del Rosario, November 2022. http://dx.doi.org/10.12804/dvcn_10336.36920_num6.

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En Colombia existen actualmente 1.391 áreas protegidas y tanto en su interior como en sus fronteras (zonas de amortiguación) se desarrollan muchas actividades humanas. El estudiante doctoral de la Facultad de Ciencias Naturales Kristian Rubiano mapeó 51 áreas protegidas para determinar las trayectorias de cambio en el uso de la tierra. Los resultados, que fueron presentados en la 58a Reunión Anual de la Asociación para la Biología Tropical y Conservación (ATBC), mostraron que las áreas protegidas están cumpliendo parcialmente su rol de conservar los ecosistemas.

Tabita, F. Robert. Biochemistry and control of the reductive tricarboxylic acid pathway of CO₂ fixation and physiological role of the Rubis CO-like protein. Office of Scientific and Technical Information (OSTI), December 2008. http://dx.doi.org/10.2172/943343.

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Academic literature on the topic 'Rubisco'

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Contents

Journal articles on the topic "Rubisco":

Dissertations / Theses on the topic "Rubisco":

Books on the topic "Rubisco":

Book chapters on the topic "Rubisco":

Conference papers on the topic "Rubisco":

Reports on the topic "Rubisco":