Structure and function of Rubisco

Andersson, Ingemar; Backlund, Anders

doi:10.1016/j.plaphy.2008.01.001

Cited by 463 publications

(433 citation statements)

References 115 publications

(165 reference statements)

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“…The chloroplast-encoded RbcL is thought to contain most of the important amino acids determining the kinetic properties of catalysis (Andersson and Backlund, 2008). Consistent with this, the specific activity of Rubisco in intergenetic hybrids shows maternal inheritance (Evans and Austin, 1986).…”

Section: Kinetic Properties Of Rubiscomentioning

confidence: 81%

“…Rubisco in higher plants is present as a multisubunit complex consisting of eight RbcL and eight RbcS: L 8 S 8 structure (Andersson and Backlund, 2008). As both the native rice and sorghum RbcS were expressed in transgenic rice, the possibility of heteropolymers of sorghum and rice Rubisco was investigated.…”

Section: Expression Of Sorghum Rbcs In Transgenic Ricementioning

confidence: 99%

“…RbcL contains most of the amino acids important for catalysis (Andersson and Backlund, 2008). By contrast, the function of RbcS is uncertain and it has been suggested that RbcS could have a role in determining the carboxylation efficiency and CO 2 specificity (Spreitzer, 2003).…”

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confidence: 99%

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Functional Incorporation of Sorghum Small Subunit Increases the Catalytic Turnover Rate of Rubisco in Transgenic Rice

et al. 2011

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Rubisco limits photosynthetic CO 2 fixation because of its low catalytic turnover rate (k cat ) and competing oxygenase reaction. Previous attempts to improve the catalytic efficiency of Rubisco by genetic engineering have gained little progress. Here we demonstrate that the introduction of the small subunit (RbcS) of high k cat Rubisco from the C 4 plant sorghum (Sorghum bicolor) significantly enhances k cat of Rubisco in transgenic rice (Oryza sativa). Three independent transgenic lines expressed sorghum RbcS at a high level, accounting for 30%, 44%, and 79% of the total RbcS. Rubisco was likely present as a chimera of sorghum and rice RbcS, and showed 1.32-to 1.50-fold higher k cat than in nontransgenic rice. Rubisco from transgenic lines showed a higher K m for CO 2 and slightly lower specificity for CO 2 than nontransgenic controls. These results suggest that Rubisco in rice transformed with sorghum RbcS partially acquires the catalytic properties of sorghum Rubisco. Rubisco content in transgenic lines was significantly increased over wild-type levels but Rubisco activation was slightly decreased. The expression of sorghum RbcS did not affect CO 2 assimilation rates under a range of CO 2 partial pressures. The J max /V cmax ratio was significantly lower in transgenic line compared to the nontransgenic plants. These observations suggest that the capacity of electron transport is not sufficient to support the increased Rubisco capacity in transgenic rice. Although the photosynthetic rate was not enhanced, the strategy presented here opens the way to engineering Rubisco for improvement of photosynthesis and productivity in the future.

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Section: Kinetic Properties Of Rubiscomentioning

confidence: 81%

Section: Expression Of Sorghum Rbcs In Transgenic Ricementioning

confidence: 99%

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Functional Incorporation of Sorghum Small Subunit Increases the Catalytic Turnover Rate of Rubisco in Transgenic Rice

et al. 2011

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“…This interpretation is consistent with previous phylogenetic analysis in which protein sequences of Rubisco Group I and Group III were inferred to form a monophyletic clade exclusive of Group II and IV (Tabita, Satagopan, et al., 2008). However, there exists an alternate hypothesis in which Group II—not Group III—is most closely related to Group I (Andersson & Backlund, 2008; Ashida et al., 2005). Given that the true evolutionary history of Rubisco cannot be observed, we are left to discriminate between these two hypotheses based on phylogenetic signal and a biophysical comparison of extant Rubisco protein species.…”

Section: Discussionmentioning

confidence: 99%

Constraining the timing of the Great Oxidation Event within the Rubisco phylogenetic tree

et al. 2017

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Ribulose 1,5‐bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO, or Rubisco) catalyzes a key reaction by which inorganic carbon is converted into organic carbon in the metabolism of many aerobic and anaerobic organisms. Across the broader Rubisco protein family, homologs exhibit diverse biochemical characteristics and metabolic functions, but the evolutionary origins of this diversity are unclear. Evidence of the timing of Rubisco family emergence and diversification of its different forms has been obscured by a meager paleontological record of early Earth biota, their subcellular physiology and metabolic components. Here, we use computational models to reconstruct a Rubisco family phylogenetic tree, ancestral amino acid sequences at branching points on the tree, and protein structures for several key ancestors. Analysis of historic substitutions with respect to their structural locations shows that there were distinct periods of amino acid substitution enrichment above background levels near and within its oxygen‐sensitive active site and subunit interfaces over the divergence between Form III (associated with anoxia) and Form I (associated with oxia) groups in its evolutionary history. One possible interpretation is that these periods of substitutional enrichment are coincident with oxidative stress exerted by the rise of oxygenic photosynthesis in the Precambrian era. Our interpretation implies that the periods of Rubisco substitutional enrichment inferred near the transition from anaerobic Form III to aerobic Form I ancestral sequences predate the acquisition of Rubisco by fully derived cyanobacterial (i.e., dual photosystem‐bearing, oxygen‐evolving) clades. The partitioning of extant lineages at high clade levels within our Rubisco phylogeny indicates that horizontal transfer of Rubisco is a relatively infrequent event. Therefore, it is possible that the mutational enrichment periods between the Form III and Form I common ancestral sequences correspond to the adaptation of key oxygen‐sensitive components of Rubisco prior to, or coincident with, the Great Oxidation Event.

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“…The resulting products, two molecules of 3-phosphoglycerate, are then used to build carbohydrates. Rubisco is a complex made of eight copies of a large subunit (RbcL), which is encoded by a chloroplast gene, and eight copies of a small subunit (RbcS), which is encoded by a nuclear gene family (Spreitzer and Salvucci, 2002;Andersson and Backlund, 2008). Although the catalytic reaction is mostly controlled by the large subunit, the small subunit also influences the reaction.…”

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confidence: 99%

Photosynthetic Trichomes Contain a Specific Rubisco with a Modified pH-Dependent Activity

et al. 2017

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ORCID IDs: 0000-0003-1551-4699 (M.P.); 0000-0002-2315-6900 (M.B.).Ribulose-1,5-biphosphate carboxylase/oxygenase (Rubisco) is the most abundant enzyme in plants and is responsible for CO 2 fixation during photosynthesis. This enzyme is assembled from eight large subunits (RbcL) encoded by a single chloroplast gene and eight small subunits (RbcS) encoded by a nuclear gene family. Rubisco is primarily found in the chloroplasts of mesophyll (C3 plants), bundlesheath (C4 plants), and guard cells. In certain species, photosynthesis also takes place in the secretory cells of glandular trichomes, which are epidermal outgrowths (hairs) involved in the secretion of specialized metabolites. However, photosynthesis and, in particular, Rubisco have not been characterized in trichomes. Here, we show that tobacco (Nicotiana tabacum) trichomes contain a specific Rubisco small subunit, NtRbcS-T, which belongs to an uncharacterized phylogenetic cluster (T). This cluster contains RbcS from at least 33 species, including monocots, many of which are known to possess glandular trichomes. Cluster T is distinct from the cluster M, which includes the abundant, functionally characterized RbcS isoforms expressed in mesophyll or bundle-sheath cells. Expression of NtRbcS-T in Chlamydomonas reinhardtii and purification of the full Rubisco complex showed that this isoform conferred higher V max and K m values as well as higher acidic pH-dependent activity than NtRbcS-M, an isoform expressed in the mesophyll. This observation was confirmed with trichome extracts. These data show that an ancient divergence allowed for the emergence of a so-far-uncharacterized RbcS cluster. We propose that secretory trichomes have a particular Rubisco uniquely adapted to secretory cells where CO 2 is released by the active specialized metabolism.

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Structure and function of Rubisco

Cited by 463 publications

References 115 publications

Functional Incorporation of Sorghum Small Subunit Increases the Catalytic Turnover Rate of Rubisco in Transgenic Rice

Functional Incorporation of Sorghum Small Subunit Increases the Catalytic Turnover Rate of Rubisco in Transgenic Rice

Constraining the timing of the Great Oxidation Event within the Rubisco phylogenetic tree

Photosynthetic Trichomes Contain a Specific Rubisco with a Modified pH-Dependent Activity

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