Rubisco regulation: a role for inhibitors

Parry, M. A. J.; Keys, A. J.; Madgwick, P. J.; Carmo‐Silva, Elizabete; Andralojc, P. J.

doi:10.1093/jxb/ern084

Cited by 253 publications

(224 citation statements)

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“…As Rubisco is inefficient due to its typical error-prone catalytic properties (Bracher et al, 179 2017), ethylene is also likely to influence protein abundance and/or activity of Rubisco activases 180 (RCAs), adding an additional layer of complexity to mediating the carboxylation process. RCAs are 181 well known as molecular chaperones for Rubisco to deal with its dead-end inhibited complexes due 182 to its high affinity for its substrate ribulose 1,5-bisphosphate and similar sugars when the active site 183 has been left unprimed with CO 2 and Mg 2+ cofactors (Parry et al, 2008 (Figure 1). The mutually antagonistic relationship between glucose and 207 ethylene signaling confers a nice example (Figure 1; Zhou et al, 1998;León and Sheen, 2003).…”

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confidence: 99%

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Ceusters

Poel

2018

Plant Physiol.

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31The volatile plant hormone ethylene plays a regulatory role in many developmental processes and in 32 biotic and abiotic stress responses. One of the under-explored actions of ethylene is its regulation of 33 photosynthesis and associated components such as stomatal conductance, chlorophyll content, light 34 reactions, carboxylation events, carbohydrate partitioning, and age-related senescence. In this 35 update, we summarize the current knowledge concerning the regulation of photosynthesis, focusing 36 on the model species Arabidopsis thaliana. We describe how ethylene directs photosynthesis in 37 juvenile non-senescing leaves and mature senescing leaves. Furthermore, we extend these insights 38 Plant Physiology Preview.

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confidence: 99%

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Ceusters

Poel

2018

Plant Physiol.

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“…One such compound is the oxygenation product 2-phosphoglycolate that needs to be repaired via photorespiration (8) and rubisco inhibitors such as xylulose 1,5-bisphosphate (XuBP) that are then dephosphorylated by specific phosphatases (9,10). XuBP, other sugar phosphates, and even rubisco's bona fide substrate ribulose 1,5-bisphosphate (RuBP) can tightly bind to the active site (11), resulting in dead-end complexes that need to be reactivated for photosynthetic CO 2 fixation to proceed. Conformational remodeling of dead-end complexes, which results in release of the inhibitor, is achieved in diverse organisms by a growing group of molecular chaperones known as the rubisco activases (Rcas) (12).…”

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confidence: 99%

Characterization of the heterooligomeric red-type rubisco activase from red algae

Loganathan

Tsai

Mueller‐Cajar

2016

Proc. Natl. Acad. Sci. U.S.A.

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The photosynthetic CO 2 -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 nuclearencoded 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.rubisco | activase | photosynthesis | AAA + proteins | red algae

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“…According to Parry et al 8 the C-terminus of RCA is important for the RuBisCO recognition and for the ATP hydrolysis, whereas the N-terminus of this protein is necessary for RuBisCO activation. 8 However, the functional role and potential targets of the short disordered binding region at the central part of the Tetraselmis RCA are unknown as of yet.…”

Section: Resultsmentioning

confidence: 99%

“…7 As a result, RuBisCO is a highly regulated machine used to control carbon fixation reaction in response of environmental fluctuations. 8 RuBisCO activase (RCA) is an enzyme responsible for the RuBisCO activation by uncoupling RuBisCO and RuBP interaction or releasing the bound RuBP or its analog from RuBisCO. 9 It allows the rapid formation of the critical carbamate in the active site of RuBisCO by binding the activator CO 2 .…”

Section: Rubisco and Rubisco Activase (Rca)mentioning

confidence: 99%

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Comparison of the intrinsic disorder propensities of the RuBisCO activase enzyme from the motile and non-motile oceanic green microalgae

Sena

Uversky

2016

Intrinsically Disordered Proteins

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Green oceanic microalgae are efficient converters of solar energy into the biomass via the photosynthesis process, with the first step of carbon fixation in the photosynthesis being controlled by the enzyme ribulose-1, 5-bisphosphate carboxylase/oxygenase (RuBisCO), which is a large proteinaceous machine composed of large (L, 52 kDa) and small (S, 12 kDa) subunits arranged as a L 8 S 8 hexadecamer that catalyzes the formation of 2 phosphoglyceric acid molecules from one ribulose 1,5-bisphosphate (RuBP) molecule and one of carbon dioxide (CO 2 ) and that is considered as the most abundant protein on Earth. The catalytic efficiency of this protein is controlled by the RuBisCO activase (RCA) that interacts with RuBisCO and promotes the CO 2 entrance to the active site of RuBisCO by removing RuBP. One of the peculiar features of RCA is the presence of functional disordered tails that might play a role in RCA-RuBisCO interaction. Based on their ability to move, microalgae are grouped into 2 major class, motile and non-motile. Motile microalgae have an obvious advantage over their non-motile counterparts because of their ability to actively migrate within the water column to find the most optimal environmental conditions. We hypothesizes that the RCA could be functionally different in the non-motile and motile microalgae. To check this hypothesis, we conducted a comparative computational analysis of the RCAs from the representatives of the non-motile (Ostreococcus tauri) and motile (Tetraselmis sp. GSL018) green oceanic microalgae.

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Rubisco regulation: a role for inhibitors

Cited by 253 publications

References 134 publications

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Ethylene Exerts Species-Specific and Age-Dependent Control of Photosynthesis

Characterization of the heterooligomeric red-type rubisco activase from red algae

Comparison of the intrinsic disorder propensities of the RuBisCO activase enzyme from the motile and non-motile oceanic green microalgae

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