Erratum: Degradation of potent Rubisco inhibitor by selective sugar phosphatase

Bracher, A.; Sharma, Anurag; Starling-Windhof, Amanda; Hartl, F. Ulrich; Hayer‐Hartl, Manajit

doi:10.1038/nplants.2015.6

Cited by 2 publications

(1 citation statement)

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“…At the same time, losing a valuable active site has reduced the capacity for carbon fixation of the host organism. RuBP is not the only inhibitory substrate, a palette of other sugar phosphates, including some generated by misfire-reactions of Rubisco itself, also tightly bind to the active site (Parry et al, 2008; Andralojc et al, 2012; Bracher et al, 2015). The affinity of the inhibitors is correlated with the enzyme's catalytic parameters, and based on the data available “superior” high specificity Rubiscos bind RuBP and other sugar phosphates more tightly than the low specificity enzymes with more flexible active sites (Pearce and Andrews, 2003; Pearce, 2006).…”

Section: The Emerging Requirement For Catalytic Chaperonesmentioning

confidence: 99%

The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites

Mueller‐Cajar

2017

Front. Mol. Biosci.

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Gaseous carbon dioxide enters the biosphere almost exclusively via the active site of the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). This highly conserved catalyst has an almost universal propensity to non-productively interact with its substrate ribulose 1,5-bisphosphate, leading to the formation of dead-end inhibited complexes. In diverse autotrophic organisms this tendency has been counteracted by the recruitment of dedicated AAA+ (ATPases associated with various cellular activities) proteins that all use the energy of ATP hydrolysis to remodel inhibited Rubisco active sites leading to release of the inhibitor. Three evolutionarily distinct classes of these Rubisco activases (Rcas) have been discovered so far. Green and red-type Rca are mostly found in photosynthetic eukaryotes of the green and red plastid lineage respectively, whereas CbbQO is associated with chemoautotrophic bacteria. Ongoing mechanistic studies are elucidating how the various motors are utilizing both similar and contrasting strategies to ultimately perform their common function of cracking the inhibited Rubisco active site. The best studied mechanism utilized by red-type Rca appears to involve transient threading of the Rubisco large subunit C-terminal peptide, reminiscent of the action performed by Clp proteases. As well as providing a fascinating example of convergent molecular evolution, Rca proteins can be considered promising crop-improvement targets. Approaches aiming to replace Rubisco in plants with improved enzymes will need to ensure the presence of a compatible Rca protein. The thermolability of the Rca protein found in crop plants provides an opportunity to fortify photosynthesis against high temperature stress. Photosynthesis also appears to be limited by Rca when light conditions are fluctuating. Synthetic biology strategies aiming to enhance the autotrophic CO2 fixation machinery will need to take into consideration the requirement for Rubisco activases as well as their properties.

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Section: The Emerging Requirement For Catalytic Chaperonesmentioning

confidence: 99%

The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites

Mueller‐Cajar

2017

Front. Mol. Biosci.

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Role of auxiliary proteins in Rubisco biogenesis and function

et al. 2015

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the conversion of atmospheric CO2 into organic compounds during photosynthesis. Despite its pivotal role in plant metabolism, Rubisco is an inefficient enzyme and has therefore been a key target in bioengineering efforts to improve crop yields. Much has been learnt about the complex cellular machinery involved in Rubisco assembly and metabolic repair over recent years. The simple form of Rubisco found in certain bacteria and dinoflagellates comprises two large subunits, and generally requires the chaperonin system for folding. However, the evolution of hexadecameric Rubisco, which comprises eight large and eight small subunits, from its dimeric precursor has rendered Rubisco in most plants, algae, cyanobacteria and proteobacteria dependent on an array of additional factors. These auxiliary factors include several chaperones for assembly as well as ATPases of the AAA+ family for functional maintenance. An integrated view of the pathways underlying Rubisco biogenesis and repair will pave the way for efforts to improve the enzyme with the goal of increasing crop yields.

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Erratum: Degradation of potent Rubisco inhibitor by selective sugar phosphatase

Cited by 2 publications

References 0 publications

The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites

The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites

Role of auxiliary proteins in Rubisco biogenesis and function

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