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Articles de revues sur le sujet « Rubisco »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 25 juillet 2025

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1

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 (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 extra

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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 (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 tra

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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 ae

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Mueller-Cajar, Oliver, and Spencer M. Whitney. "Evolving improved Synechococcus Rubisco functional expression in Escherichia coli." Biochemical Journal 414, no. 2 (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-Blu

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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 (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), s

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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 (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 w

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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 (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 intera

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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 (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 deplet

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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 (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 encod

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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 (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, catalyz

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Whitney, Spencer M., Rosemary Birch, Celine Kelso, Jennifer L. Beck, and Maxim V. Kapralov. "Improving recombinant Rubisco biogenesis, plant photosynthesis and growth by coexpressing its ancillary RAF1 chaperone." Proceedings of the National Academy of Sciences 112, no. 11 (2015): 3564–69. http://dx.doi.org/10.1073/pnas.1420536112.

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Enabling improvements to crop yield and resource use by enhancing the catalysis of the photosynthetic CO2-fixing enzyme Rubisco has been a longstanding challenge. Efforts toward realization of this goal have been greatly assisted by advances in understanding the complexities of Rubisco’s biogenesis in plastids and the development of tailored chloroplast transformation tools. Here we generate transplastomic tobacco genotypes expressing Arabidopsis Rubisco large subunits (AtL), both on their own (producing tobAtL plants) and with a cognate Rubisco accumulation factor 1 (AtRAF1) chaperone (produc

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Elsaied, Hosam, and Takeshi Naganuma. "Phylogenetic Diversity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Large-Subunit Genes from Deep-Sea Microorganisms." Applied and Environmental Microbiology 67, no. 4 (2001): 1751–65. http://dx.doi.org/10.1128/aem.67.4.1751-1765.2001.

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ABSTRACT The phylogenetic diversity of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO, E.C. 4.1.1.39) large-subunit genes of deep-sea microorganisms was analyzed. Bulk genomic DNA was isolated from seven samples, including samples from the Mid-Atlantic Ridge and various deep-sea habitats around Japan. The kinds of samples were hydrothermal vent water and chimney fragment; reducing sediments from a bathyal seep, a hadal seep, and a presumed seep; and symbiont-bearing tissues of the vent mussel, Bathymodiolus sp., and the seep vestimentiferan tubeworm, Lamellibrachia sp. The RuBisC

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Rydzy, Małgorzata, Michał Tracz, Andrzej Szczepaniak, and Joanna Grzyb. "Insights into the Structure of Rubisco from Dinoflagellates-in Silico Studies." International Journal of Molecular Sciences 22, no. 16 (2021): 8524. http://dx.doi.org/10.3390/ijms22168524.

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is one of the best studied enzymes. It is crucial for photosynthesis, and thus for all of biosphere’s productivity. There are four isoforms of this enzyme, differing by amino acid sequence composition and quaternary structure. However, there is still a group of organisms, dinoflagellates, single-cell eukaryotes, that are confirmed to possess Rubisco, but no successful purification of the enzyme of such origin, and hence a generation of a crystal structure was reported to date. Here, we are using in silico tools to generate the possible

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Morell, MK, K. Paul, HJ Kane, and TJ Andrews. "Rubisco: Maladapted or Misunderstood." Australian Journal of Botany 40, no. 5 (1992): 431. http://dx.doi.org/10.1071/bt9920431.

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Life depends on a single enzyme, D-ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco), for the acquisition of essentially all of its carbon. Applying Darwinian principles, one would expect this enzyme to have been rigorously selected for speed and accuracy, and it is a surprise to discover that, even in its most highly developed forms, it is both slow and confused. This review looks for clues about the causes of Rubisco's slow evolutionary refinement in its complex catalytic chemistry and in its tendency to catalyse abortive side reactions. We assess the possibilities for improving Rubi

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Valegård, Karin, Dirk Hasse, Inger Andersson, and Laura H. Gunn. "Structure of Rubisco fromArabidopsis thalianain complex with 2-carboxyarabinitol-1,5-bisphosphate." Acta Crystallographica Section D Structural Biology 74, no. 1 (2018): 1–9. http://dx.doi.org/10.1107/s2059798317017132.

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The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fromArabidopsis thalianais reported at 1.5 Å resolution. In light of the importance ofA. thalianaas a model organism for understanding higher plant biology, and the pivotal role of Rubisco in photosynthetic carbon assimilation, there has been a notable absence of anA. thalianaRubisco crystal structure.A. thalianaRubisco is an L8S8hexadecamer comprising eight plastome-encoded catalytic large (L) subunits and eight nuclear-encoded small (S) subunits.A. thalianaproduces four distinct small-subunit isoforms (RbcS1A,

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Wei, Xueming, Luis A. Sayavedra-Soto, and Daniel J. Arp. "The transcription of the cbb operon in Nitrosomonas europaea." Microbiology 150, no. 6 (2004): 1869–79. http://dx.doi.org/10.1099/mic.0.26785-0.

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Nitrosomonas europaea is an aerobic ammonia-oxidizing bacterium that participates in the C and N cycles. N. europaea utilizes CO2 as its predominant carbon source, and is an obligate chemolithotroph, deriving all the reductant required for energy and biosynthesis from the oxidation of ammonia (NH3) to nitrite (). This bacterium fixes carbon via the Calvin–Benson–Bassham (CBB) cycle via a type I ribulose bisphosphate carboxylase/oxygenase (RubisCO). The RubisCO operon is composed of five genes, cbbLSQON. This gene organization is similar to that of the operon for ‘green-like’ type I RubisCOs in

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Poudel, Saroj, Douglas H. Pike, Hagai Raanan, et al. "Biophysical analysis of the structural evolution of substrate specificity in RuBisCO." Proceedings of the National Academy of Sciences 117, no. 48 (2020): 30451–57. http://dx.doi.org/10.1073/pnas.2018939117.

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Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the most abundant enzyme on Earth. However, its catalytic rate per molecule of protein is extremely slow and the binding of the primary substrate, CO2, is competitively displaced by O2.Hence, carbon fixation by RuBisCO is highly inefficient; indeed, in higher C3 plants, about 30% of the time the enzyme mistakes CO2for O2. Using genomic and structural analysis, we identify regions around the catalytic site that play key roles in discriminating between CO2and O2. Our analysis identified positively charged cavities directly around the a

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Baker, Stefanie H., Songmu Jin, Henry C. Aldrich, Gary T. Howard, and Jessup M. Shively. "Insertion Mutation of the Form I cbbL Gene Encoding Ribulose Bisphosphate Carboxylase/Oxygenase (RuBisCO) in Thiobacillus neapolitanus Results in Expression of Form II RuBisCO, Loss of Carboxysomes, and an Increased CO2 Requirement for Growth." Journal of Bacteriology 180, no. 16 (1998): 4133–39. http://dx.doi.org/10.1128/jb.180.16.4133-4139.1998.

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ABSTRACT It has been previously established that Thiobacillus neapolitanus fixes CO2 by using a form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO), that much of the enzyme is sequestered into carboxysomes, and that the genes for the enzyme, cbbL and cbbS, are part of a putative carboxysome operon. In the present study, cbbL andcbbS were cloned and sequenced. Analysis of RNA showed thatcbbL and cbbS are cotranscribed on a message approximately 2,000 nucleotides in size. The insertion of a kanamycin resistance cartridge into cbbL resulted in a premature termination of transcription; a

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Young, J. N., R. E. M. Rickaby, M. V. Kapralov, and D. A. Filatov. "Adaptive signals in algal Rubisco reveal a history of ancient atmospheric carbon dioxide." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1588 (2012): 483–92. http://dx.doi.org/10.1098/rstb.2011.0145.

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Rubisco, the most abundant enzyme on the Earth and responsible for all photosynthetic carbon fixation, is often thought of as a highly conserved and sluggish enzyme. Yet, different algal Rubiscos demonstrate a range of kinetic properties hinting at a history of evolution and adaptation. Here, we show that algal Rubisco has indeed evolved adaptively during ancient and distinct geological periods. Using DNA sequences of extant marine algae of the red and Chromista lineage, we define positive selection within the large subunit of Rubisco, encoded by rbcL , to occur basal to the radiation of moder

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Raven, John A., Mario Giordano, John Beardall, and Stephen C. Maberly. "Algal evolution in relation to atmospheric CO 2 : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1588 (2012): 493–507. http://dx.doi.org/10.1098/rstb.2011.0212.

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Oxygenic photosynthesis evolved at least 2.4 Ga; all oxygenic organisms use the ribulose bisphosphate carboxylase-oxygenase (Rubisco)–photosynthetic carbon reduction cycle (PCRC) rather than one of the five other known pathways of autotrophic CO 2 assimilation. The high CO 2 and (initially) O 2 -free conditions permitted the use of a Rubisco with a high maximum specific reaction rate. As CO 2 decreased and O 2 increased, Rubisco oxygenase activity increased and 2-phosphoglycolate was produced, with the evolution of pathways recycling this inhibitory product to sugar phosphates. Changed atmosph

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Schulz, Luca, Zhijun Guo, Jan Zarzycki, et al. "Evolution of increased complexity and specificity at the dawn of form I Rubiscos." Science 378, no. 6616 (2022): 155–60. http://dx.doi.org/10.1126/science.abq1416.

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The evolution of ribulose-1,5-bisphosphate carboxylase/oxygenases (Rubiscos) that discriminate strongly between their substrate carbon dioxide and the undesired side substrate dioxygen was an important event for photosynthetic organisms adapting to an oxygenated environment. We use ancestral sequence reconstruction to recapitulate this event. We show that Rubisco increased its specificity and carboxylation efficiency through the gain of an accessory subunit before atmospheric oxygen was present. Using structural and biochemical approaches, we retrace how this subunit was gained and became esse

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Karthick, Palanivelu Vikram, Alagarswamy Senthil, Maduraimuthu Djanaguiraman, et al. "Improving Crop Yield through Increasing Carbon Gain and Reducing Carbon Loss." Plants 13, no. 10 (2024): 1317. http://dx.doi.org/10.3390/plants13101317.

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Photosynthesis is a process where solar energy is utilized to convert atmospheric CO2 into carbohydrates, which forms the basis for plant productivity. The increasing demand for food has created a global urge to enhance yield. Earlier, the plant breeding program was targeting the yield and yield-associated traits to enhance the crop yield. However, the yield cannot be further improved without improving the leaf photosynthetic rate. Hence, in this review, various strategies to enhance leaf photosynthesis were presented. The most promising strategies were the optimization of Rubisco carboxylatio

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Toyoda, Koichi, Yoichi Yoshizawa, Hiroyuki Arai, Masaharu Ishii, and Yasuo Igarashi. "The role of two CbbRs in the transcriptional regulation of three ribulose-1,5-bisphosphate carboxylase/oxygenase genes in Hydrogenovibrio marinus strain MH-110." Microbiology 151, no. 11 (2005): 3615–25. http://dx.doi.org/10.1099/mic.0.28056-0.

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Hydrogenovibrio marinus MH-110 possesses three different sets of genes for ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO): two form I (cbbLS-1 and cbbLS-2) and one form II (cbbM). We have previously shown that the expression of these RubisCO genes is dependent on the ambient CO2 concentration. LysR-type transcriptional regulators, designated CbbR1 and CbbRm, are encoded upstream of the cbbLS-1 and cbbM genes, respectively. In this study, we revealed by gel shift assay that CbbR1 and CbbRm bind with higher affinity to the promoter regions of cbbLS-1 and cbbM, respectively, and with l

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Waheeda, Kazi, and Po-Lin Chiu. "Complex formation of rubisco and rubisco activase." Biophysical Journal 121, no. 3 (2022): 452a. http://dx.doi.org/10.1016/j.bpj.2021.11.520.

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Sage, Rowan F., Danielle A. Way, and David S. Kubien. "Rubisco, Rubisco activase, and global climate change." Journal of Experimental Botany 59, no. 7 (2008): 1581–95. http://dx.doi.org/10.1093/jxb/ern053.

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Portis, A. R. "The regulation of Rubisco by Rubisco activase." Journal of Experimental Botany 46, special (1995): 1285–91. http://dx.doi.org/10.1093/jxb/46.special_issue.1285.

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Singh, Jaya, and F. Robert Tabita. "Roles of RubisCO and the RubisCO-Like Protein in 5-Methylthioadenosine Metabolism in the Nonsulfur Purple Bacterium Rhodospirillum rubrum." Journal of Bacteriology 192, no. 5 (2009): 1324–31. http://dx.doi.org/10.1128/jb.01442-09.

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ABSTRACT Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the assimilation of atmospheric CO2 into organic matter and is thus central to the existence of life on earth. The beginning of the 2000s was marked by the discovery of a new family of proteins, the RubisCO-like proteins (RLPs), which are structural homologs of RubisCO. RLPs are unable to catalyze CO2 fixation. The RLPs from Chlorobaculum tepidum, Bacillus subtilis, Geobacillus kaustophilus, and Microcystis aeruginosa have been shown to participate in sulfur metabolism. Whereas the precise function of C. tepidum RLP i

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Yoshizawa, Yoichi, Koichi Toyoda, Hiroyuki Arai, Masaharu Ishii, and Yasuo Igarashi. "CO2-Responsive Expression and Gene Organization of Three Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Enzymes and Carboxysomes in Hydrogenovibrio marinus Strain MH-110." Journal of Bacteriology 186, no. 17 (2004): 5685–91. http://dx.doi.org/10.1128/jb.186.17.5685-5691.2004.

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ABSTRACT Hydrogenovibrio marinus strain MH-110, an obligately lithoautotrophic hydrogen-oxidizing bacterium, fixes CO2 by the Calvin-Benson-Bassham cycle. Strain MH-110 possesses three different sets of genes for ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO): CbbLS-1 and CbbLS-2, which belong to form I (L8S8), and CbbM, which belongs to form II (Lx). In this paper, we report that the genes for CbbLS-1 (cbbLS-1) and CbbM (cbbM) are both followed by the cbbQO genes and preceded by the cbbR genes encoding LysR-type regulators. In contrast, the gene for CbbLS-2 (cbbLS-2) is followed by

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Xiang, Fu, Yuanping Fang, and Jun Xiang. "Structural and evolutionary relationships among RuBisCOs inferred from their large and small subunits." Zeitschrift für Naturforschung C 71, no. 5-6 (2016): 181–89. http://dx.doi.org/10.1515/znc-2016-0014.

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Abstract Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the key enzyme to assimilate CO2 into the biosphere. The nonredundant structural data sets for three RuBisCO domain superfamilies, i.e. large subunit C-terminal domain (LSC), large subunit N-terminal domain (LSN) and small subunit domain (SS), were selected using QR factorization based on the structural alignment with QH as the similarity measure. The structural phylogenies were then constructed to investigate a possible functional significance of the evolutionary diversification. The LSC could have occurred in both bacteria

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Hotto, Amber M., Coralie Salesse-Smith, Myat Lin, Florian A. Busch, Isabelle Simpson, and David B. Stern. "Rubisco production in maize mesophyll cells through ectopic expression of subunits and chaperones." Journal of Experimental Botany 72, no. 13 (2021): 4930–37. http://dx.doi.org/10.1093/jxb/erab189.

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Abstract C4 plants, such as maize, strictly compartmentalize Rubisco to bundle sheath chloroplasts. The molecular basis for the restriction of Rubisco from the more abundant mesophyll chloroplasts is not fully understood. Mesophyll chloroplasts transcribe the Rubisco large subunit gene and, when normally quiescent transcription of the nuclear Rubisco small subunit gene family is overcome by ectopic expression, mesophyll chloroplasts still do not accumulate measurable Rubisco. Here we show that a combination of five ubiquitin promoter-driven nuclear transgenes expressed in maize leads to mesoph

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Demirevska-Kepova, Klimentina, and Urs Feller. "Heat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants." Acta Physiologiae Plantarum 26, no. 1 (2004): 103–14. http://dx.doi.org/10.1007/s11738-004-0050-7.

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Madhavan, S., M. S. Miller-Goodman, and K. W. Lee. "Immunolocalization of Rubisco Activase and Rubisco in C3 and C4 Plant Tissues." Microscopy and Microanalysis 6, S2 (2000): 472–73. http://dx.doi.org/10.1017/s1431927600034851.

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Ribulose bisphosphate carboxylase/oxygenase (Rubisco), an abundant enzyme in chloroplasts, must be activated by CO2 in order for it to catalyze the carboxylation of ribulose bisphosphate. Rubisco activase, a nuclear encoded chloroplast protein was first identified as a biochemical lesion in the rca mutant of Arabidopsis (1) which lacked this enzyme. Study of Rubisco in this mutant (2) and transgenic tobacco plants with reduced Rubisco activase levels showed that Rubisco could not achieve and maintain an adequate level of activity, in vivo, without an activase. Rubisco activase promotes ‘activa

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Feng, Yujiao, Hao Wu, Huanhuan Liu, Yonghui He, and Zhitong Yin. "Effects of OsRCA Overexpression on Rubisco Activation State and Photosynthesis in Maize." Plants 12, no. 8 (2023): 1614. http://dx.doi.org/10.3390/plants12081614.

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Ribulose–1,5–bisphosphate carboxylase/oxygenase (Rubisco) is the rate–limiting enzyme for photosynthesis. Rubisco activase (RCA) can regulate the Rubisco activation state, influencing Rubisco activity and photosynthetic rate. We obtained transgenic maize plants that overproduced rice RCA (OsRCAOE) and evaluated photosynthesis in these plants by measuring gas exchange, energy conversion efficiencies in photosystem (PS) I and PSII, and Rubisco activity and activation state. The OsRCAOE lines showed significantly higher initial Rubisco activity and activation state, net photosynthetic rate, and P

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SEVİNDİK, Emre. "Amino Acids Sequence Based in Silico Analysis of RuBisCO (Ribulose-1,5 Bisphosphate Carboxylase Oxygenase) Proteins in Some Carthamus L. ssp." Notulae Scientia Biologicae 9, no. 2 (2017): 204–8. http://dx.doi.org/10.15835/nsb9210053.

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RuBisCO is an important enzyme for plants to photosynthesize and balance carbon dioxide in the atmosphere. This study aimed to perform sequence, physicochemical, phylogenetic and 3D (three-dimensional) comparative analyses of RuBisCO proteins in the Carthamus ssp. using various bioinformatics tools. The sequence lengths of the RuBisCO proteins were between 166 and 477 amino acids, with an average length of 411.8 amino acids. Their molecular weights (Mw) ranged from 18711.47 to 52843.09 Da; the most acidic and basic protein sequences were detected in C. tinctorius (pI = 5.99) and in C. tenuis (

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Witte, Brian, David John, Boris Wawrik, John H. Paul, David Dayan, and F. Robert Tabita. "Functional Prokaryotic RubisCO from an Oceanic Metagenomic Library." Applied and Environmental Microbiology 76, no. 9 (2010): 2997–3003. http://dx.doi.org/10.1128/aem.02661-09.

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ABSTRACT Culture-independent studies have indicated that there is significant diversity in the ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) enzymes used by marine, freshwater, and terrestrial autotrophic bacteria. Surprisingly, little is known about the catalytic properties of many environmentally significant RubisCO enzymes. Because one of the goals of RubisCO research is to somehow modify or select for RubisCO molecules with improved kinetic properties, a facile means to isolate functional and novel RubisCO molecules directly from the environment was developed. In this report, w

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Suganami, Mao, Yuji Suzuki, Eri Kondo, Shinji Nishida, So Konno, and Amane Makino. "Effects of Overproduction of Rubisco Activase on Rubisco Content in Transgenic Rice Grown at Different N Levels." International Journal of Molecular Sciences 21, no. 5 (2020): 1626. http://dx.doi.org/10.3390/ijms21051626.

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It has been reported that overproduction of Rubisco activase (RCA) in rice (Oryza sativa L.) decreased Rubisco content, resulting in declining photosynthesis. We examined the effects of RCA levels on Rubisco content using transgenic rice with overexpressed or suppressed RCA under the control of different promoters of the RCA and Rubisco small subunit (RBCS) genes. All plants were grown hydroponically with different N concentrations (0.5, 2.0 and 8.0 mM-N). In RCA overproduced plants with > 2-fold RCA content (RCA-HI lines), a 10%–20% decrease in Rubisco content was observed at 0.5 and 2.0 m

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Warren, Charles R., Mark A. Adams, and ZuLiang Chen. "Is photosynthesis related to concentrations of nitrogen and Rubisco in leaves of Australian native plants?" Functional Plant Biology 27, no. 5 (2000): 407. http://dx.doi.org/10.1071/pp98162.

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The relationships among light-saturated photosynthesis and concentrations of nitrogen and ribulose-1,5- bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39) in Australian native plants are poorly known, primarily due to the difficulty of extracting and analysing Rubisco from such species. Rubisco may be rapidly quantified in crude extracts of plant tissue by capillary electrophoresis (CE); however, the presence of phenolic compounds in many Australian native plants limits the use of these methods. The addition of insoluble polyvinylpolypyrrolidone (PVPP) during leaf extractions effectivel

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Yokota, Akiho. "Revisiting RuBisCO." Bioscience, Biotechnology, and Biochemistry 81, no. 11 (2017): 2039–49. http://dx.doi.org/10.1080/09168451.2017.1379350.

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Portis, Archie R. "Rubisco activase." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1015, no. 1 (1990): 15–28. http://dx.doi.org/10.1016/0005-2728(90)90211-l.

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Raunser, S., R. Magnani, Z. Huang, et al. "Rubisco in complex with Rubisco large subunit methyltransferase." Proceedings of the National Academy of Sciences 106, no. 9 (2009): 3160–65. http://dx.doi.org/10.1073/pnas.0810563106.

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Cheng, Lailiang, and Leslie H. Fuchigami. "Photometric Measurements of Rubisco Activity in Leaves of Deciduous Fruit Crops." HortScience 32, no. 3 (1997): 531A—531. http://dx.doi.org/10.21273/hortsci.32.3.531a.

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Ribulose bisphosphate carboxylase/oxygenase (Rubisco) initiates the photosynthetic carbon metabolism;therefore, its activity has been measured in many physiological studies. However, information on in vitro Rubisco activity from leaves of deciduous fruit crops is very limited and the reported activities are suspiciously low. We measured Rubisco activity in crude extracts of leaves of apple, pear, peach, cherry, and grape by using a photometric method in which RuBP carboxylation was enzymically coupled to NADH oxidation. Replacing polyvinylpyrrolidone with polyvinylpolypyrrolidone in the extrac

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Watson, Gregory M. F., Jae-Pil Yu, and F. Robert Tabita. "Unusual Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase of Anoxic Archaea." Journal of Bacteriology 181, no. 5 (1999): 1569–75. http://dx.doi.org/10.1128/jb.181.5.1569-1575.1999.

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ABSTRACT The predominant pool of organic matter on earth is derived from the biological reduction and assimilation of carbon dioxide gas, catalyzed primarily by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). By virtue of its capacity to use molecular oxygen as an alternative and competing gaseous substrate, the catalytic efficiency of RubisCO and the enzyme’s ability to assimilate CO2 may be severely limited, with consequent environmental and agricultural effects. Recent genomic sequencing projects, however, have identified putative RubisCO genes from anoxic Archaea. In

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S.M., Bayramov. "Rubisco Activase: Structure, Expression And Regulation Role." Journal of Life Sciences and Biomedicine 69, no. 2 (2014): 115–22. https://doi.org/10.5281/zenodo.7436737.

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Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase uses the energy from ATP hydrolysis to remove tight binding inhibitors from Rubisco, thus playing a key role in regulating photosynthesis in plants. Being one of the most common enzymes in the nature Rubisco activase activates Rubisco, which is the catalizator of the primary reaction of CO2 assimilation and plays an important role in the regulation of plant growth. The review provides information on the role of Rubisco activase in the recovery of Rubisco catalytic activity, structural and functional composition of the enzyme, duirn

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MARTÍNEZ-BARAJAS, E., J. MOLINA-GALÁN, and E. SÁNCHEZ de JIMÉNEZ. "Regulation of Rubisco activity during grain-fill in maize: possible role of Rubisco activase." Journal of Agricultural Science 128, no. 2 (1997): 155–61. http://dx.doi.org/10.1017/s002185969600408x.

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Levels of ribulose bisphosphate carboxylase (Rubisco) and Rubisco activase were compared in leaves above the ear in two genetically related populations (Z0 and Z20) of maize (Zea mays L.). Z20 was obtained from Z0 after twenty agronomic selection cycles for grain yield improvement (c. 90% above Z0). Plants were cultivated in the highlands of Mexico and leaves were sampled weekly during the grain-filling period. Chlorophyll, soluble protein and Rubisco activity were measured. Chlorophyll and soluble protein content slowly decreased during this period, the former faster than the latter, with no

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Cheng, Lailiang, and Leslie H. Fuchigami. "The Relationship between Rubisco Activity and Photosynthesis in Apple Leaves with Different Nitrogen Content." HortScience 32, no. 3 (1997): 530E—531. http://dx.doi.org/10.21273/hortsci.32.3.530e.

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Based on the curvilinear relationship between carboxylation efficiency and leaf N in apple leaves, we hypothesized that deactivation of Rubisco accounts for the lack of response of photosynthesis to increasing leaf N under high N supply. A wide range of leaf N content (from 1.0 to 5.0 g·m–2) was achieved by fertigating bench-grafted Fuji/M26 apple trees for 6 weeks with different N concentrations using a modified Hoagland solution. Analysis of photosynthesis in response to intercellular CO2 under both 21% and 2% O2 indicated that photosynthesis at ambient CO2 was mainly determined by the activ

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O'Leary, Brendan M., Andrew P. Scafaro, Ricarda Fenske, et al. "Rubisco lysine acetylation occurs at very low stoichiometry in mature Arabidopsis leaves: implications for regulation of enzyme function." Biochemical Journal 477, no. 19 (2020): 3885–96. http://dx.doi.org/10.1042/bcj20200413.

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Multiple studies have shown ribulose-1,5-bisphosphate carboxylase/oxygenase (E.C. 4.1.1.39; Rubisco) to be subject to Lys-acetylation at various residues; however, opposing reports exist about the biological significance of these post-translational modifications. One aspect of the Lys-acetylation that has not been addressed in plants generally, or with Rubisco specifically, is the stoichiometry at which these Lys-acetylation events occur. As a method to ascertain which Lys-acetylation sites on Arabidopsis Rubisco might be of regulatory importance to its catalytic function in the Calvin–Benson

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Tabita, F. Robert, Thomas E. Hanson, Sriram Satagopan, Brian H. Witte, and Nathan E. Kreel. "Phylogenetic and evolutionary relationships of RubisCO and the RubisCO-like proteins and the functional lessons provided by diverse molecular forms." Philosophical Transactions of the Royal Society B: Biological Sciences 363, no. 1504 (2008): 2629–40. http://dx.doi.org/10.1098/rstb.2008.0023.

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Ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RubisCO) catalyses the key reaction by which inorganic carbon may be assimilated into organic carbon. Phylogenetic analyses indicate that there are three classes of bona fide RubisCO proteins, forms I, II and III, which all catalyse the same reactions. In addition, there exists another form of RubisCO, form IV, which does not catalyse RuBP carboxylation or oxygenation. Form IV is actually a homologue of RubisCO and is called the RubisCO-like protein (RLP). Both RubisCO and RLP appear to have evolved from an ancestor protein in a methanoge

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Guo, Xue, Huaqun Yin, Jing Cong, Zhimin Dai, Yili Liang, and Xueduan Liu. "RubisCO Gene Clusters Found in a Metagenome Microarray from Acid Mine Drainage." Applied and Environmental Microbiology 79, no. 6 (2013): 2019–26. http://dx.doi.org/10.1128/aem.03400-12.

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ABSTRACTThe enzyme responsible for carbon dioxide fixation in the Calvin cycle, ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO), is always detected as a phylogenetic marker to analyze the distribution and activity of autotrophic bacteria. However, such an approach provides no indication as to the significance of genomic content and organization. Horizontal transfers of RubisCO genes occurring in eubacteria and plastids may seriously affect the credibility of this approach. Here, we presented a new method to analyze the diversity and genomic content of RubisCO genes in acid mine drain

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Khaembah, Edith N., François Gastal, Serge Carre, Louis J. Irving, Philippe Barre, and Cory Matthew. "Morphology and Rubisco turnover characteristics of perennial ryegrass breeding populations after two and four cycles of divergent selection for long or short leaf length." Crop and Pasture Science 64, no. 7 (2013): 687. http://dx.doi.org/10.1071/cp13066.

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Perennial ryegrass populations previously subjected to two or four cycles of selection for short or long leaf length were studied to determine the response of morphological traits to selection and interaction to determine yield. Measured morphological traits were leaf length, leaf appearance interval, ligule appearance interval, leaf elongation duration, leaf elongation rate, tiller number, tiller dry weight, and herbage dry matter. Additionally, Rubisco concentration during leaf development was measured to determine the association of Rubisco turnover with morphological characteristics and yi

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Woodrow, IE, ME Kelly, and KA Mott. "Limitation of the Rate of Ribulosebisphosphate Carboxylase Activation by Carbamylation and Ribulosebisphosphate Carboxylase Activase Activity: Development and Tests of a Mechanistic Model." Functional Plant Biology 23, no. 2 (1996): 141. http://dx.doi.org/10.1071/pp9960141.

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A mechanistically-based model of light-mediated activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is developed. The model describes the kinetics of Rubisco activation following a relatively rapid increase in photon flux density (PPFD) from an initially low level. Underlying the model is the assumption that there are two slow processes that could potentially limit the rate of light-mediated Rubisco activation. These processes are the addition of the activator CO2 to the large subunit of Rubisco, which is accompanied by a conformational change in the enzyme (carbamylation),

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