Unraveling Rubisco packaging within β-carboxysomes.

In this issue of Structure, Kong et al. utilized cryoelectron tomography to closely examine Rubisco packaging within β-carboxysomes. They observed unique Rubisco packaging arrangements that may have important implications for carboxysome structural integrity.

Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.

Cyanobacterial CO concentrating mechanisms (CCMs) sequester a globally consequential proportion of carbon into the biosphere. Proteinaceous microcompartments, called carboxysomes, play a critical role in CCM function, housing two enzymes to enhance CO fixation: carbonic anhydrase (CA) and Rubisco. Despite its importance, our current understanding of the carboxysomal CAs found in α-cyanobacteria, CsoSCA, remains limited, particularly regarding the regulation of its activity.

A carboxysome-based CO concentrating mechanism for C crop chloroplasts: advances and the road ahead.

The introduction of the carboxysome-based CO concentrating mechanism (CCM) into crop plants has been modelled to significantly increase crop yields. This projection serves as motivation for pursuing this strategy to contribute to global food security. The successful implementation of this engineering challenge is reliant upon the transfer of a microcompartment that encapsulates cyanobacterial Rubisco, known as the carboxysome, alongside active bicarbonate transporters.

Plant-based carboxysomes: another step toward increased crop yields.

Synthetically reconstructed carboxysomes form the basis of CO-concentrating mechanisms (CCMs) that could enhance the photosynthetic efficiency of crops and improve yield. Recently, Chen et al. revealed another step toward the reconstruction of bacterial carboxysomes in plants, reporting the formation of almost-complete carboxysomes in the chloroplast of Nicotiana tabacum.

Towards engineering a hybrid carboxysome.

Carboxysomes are bacterial microcompartments, whose structural features enable the encapsulated Rubisco holoenzyme to operate in a high-CO environment. Consequently, Rubiscos housed within these compartments possess higher catalytic turnover rates relative to their plant counterparts. This particular enzymatic property has made the carboxysome, along with associated transporters, an attractive prospect to incorporate into plant chloroplasts to increase future crop yields.

A new method to visualize CEP hormone-CEP receptor interactions in vascular tissue in vivo.

C-TERMINALLY ENCODED PEPTIDEs (CEPs) control diverse responses in plants including root development, root system architecture, nitrogen demand signalling, and nutrient allocation that influences yield, and there is evidence that different ligands impart different phenotypic responses. Thus, there is a need for a simple method that identifies bona fide CEP hormone-receptor pairings in vivo and examines whether different CEP family peptides bind the same receptor. We used formaldehyde or photoactivation to cross-link fluorescently tagged group 1 or group 2 CEPs to receptors in semi-purified Medicago truncatula or Arabidopsis thaliana leaf vascular tissues to verify that COMPACT ROOT ARCHITECTURE 2 (CRA2) is the Medicago CEP receptor, and to investigate whether sequence diversity within the CEP family influences receptor binding.

Rubisco proton production can drive the elevation of CO within condensates and carboxysomes.

Membraneless organelles containing the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) are a common feature of organisms utilizing CO concentrating mechanisms to enhance photosynthetic carbon acquisition. In cyanobacteria and proteobacteria, the Rubisco condensate is encapsulated in a proteinaceous shell, collectively termed a carboxysome, while some algae and hornworts have evolved Rubisco condensates known as pyrenoids. In both cases, CO fixation is enhanced compared with the free enzyme.