Insights into eukaryotic Rubisco assembly — Crystal structures of RbcX chaperones from Arabidopsis thaliana

Kolesinski, Piotr; Golik, Przemysław; Grudnik, P.; Piechota, Janusz; Markiewicz, Michał; Tarnawski, Mirosław; Dubin, Grzegorz; Szczepaniak, Andrzej

doi:10.1016/j.bbagen.2012.12.025

Cited by 21 publications

(22 citation statements)

References 34 publications

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“…Finally, binding of RbcS displaces Raf1 and completes assembly of the holoenzyme. Like the structurally unrelated Rubisco-assembly chaperone RbcX 16,32,33 , Raf1 is dimeric and engages in bivalent interactions with RbcL, a principle that probably relates to the antiparallel RbcL dimer being the building block of the RbcL 8 complex. As shown by X-ray crystallographic analysis, Raf1 consists of an N-terminal α-domain, a flexible linker segment and a C-terminal β-sheet domain that mediates dimerization.…”

Section: Discussionmentioning

confidence: 99%

Structure and mechanism of the Rubisco-assembly chaperone Raf1

Hauser

Bhat

Miličić

et al. 2015

Nat Struct Mol Biol

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Biogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of ∼40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a β-sheet dimerization domain and a flexibly linked α-helical domain. Chemical cross-linking and EM reconstruction indicate that the β-domains bind along the equator of each RbcL2 unit, and the α-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.

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Section: Discussionmentioning

confidence: 99%

Structure and mechanism of the Rubisco-assembly chaperone Raf1

Hauser

Bhat

Miličić

et al. 2015

Nat Struct Mol Biol

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“…Once the large subunit is properly folded, assembly factors such as RBCX, RAF1, and BSD2 help the transition from L 2 dimers and L 8 core to functional L 8 S 8 complexes (Aigner et al., ; Feiz et al., ; Hauser et al., ; Kolesinski, Belusiak, Czarnocki‐Cieciura, & Szczepaniak, ; Kolesinski et al., ; Liu et al., ; Saschenbrecker et al., ). In a recent study, co‐expression of the large subunit and RAF1 from Arabidopsis in tobacco chloroplasts has shown that Rubisco from higher plants prefers native RAF1 for efficient assembly (Whitney et al., ).…”

Section: Discussionmentioning

confidence: 99%

Red algal Rubisco fails to accumulate in transplastomic tobacco expressing Griffithsia monilis RbcL and RbcS genes

Lin

Hanson

2018

Plant Direct

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In C 3 plants, the carbon fixation step catalyzed by ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) represents a major rate-limiting step due to the competing oxygenation reaction, which leads to the energy-intensive photorespiration and lowers the overall photosynthetic efficiency. Hence, there is great biotechnological interest in replacing the Rubisco in C 3 crops with a more efficient enzyme. The Rubisco enzymes from red algae are among the most attractive choices due to their remarkable preference for carboxylation over oxygenation reaction. However, the biogenesis of Rubisco is extremely complex. The Rubisco enzymes in plants, algae, and cyanobacteria are made up of eight large and eight small subunits. The folding of the large subunits and the assembly of the large subunits with the small subunits to form a functional holoenzyme require specific chaperonin complexes and assembly factors. As a result, previous success in expressing foreign Rubisco in plants has been limited to Rubisco large subunits from closely related plant species and simpler bacterial enzymes. In our previous work, we successfully replaced the Rubisco in tobacco with a cyanobacterial enzyme, which was able to support the phototrophic growth of the transgenic plants. In this work, we used the same approach to express the Rubisco subunits from the red alga Griffithsia monilis in tobacco chloroplasts in the absence of the tobacco Rubisco large subunit.Although the red algal Rubisco genes are being transcribed in tobacco chloroplasts, the transgenic plants lack functional Rubisco and can only grow in a medium containing sucrose. Our results suggest that co-expression of compatible chaperones will be necessary for successful assembly of red algal Rubisco in plants. K E Y W O R D Schloroplast transformation, Griffithsia monilis, photosynthesis, Rubisco

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“…A close coupling between chaperonin folding of RbcL and further assembly, mediated by an additional chloroplast chaperone, RbcX, was subsequently revealed in some types of cyanobacteria [63][64][65][66][67][68]. In Arabidopsis as well, two homologs of this protein are expressed and have a similar structure and function to the cyanobacterial protein [69,70]. Additional factors were described in maize, such as BUNDLE SHEATH DEFECTIVE 2 (BSD2) [71] and RUBISCO ACCUMU-LATION FACTOR 1 (RAF1), which were shown to be necessary for full assembly of functional Rubisco in this plant [62].…”

Section: Trends In Plant Sciencementioning

confidence: 99%