Protein-based organelles in bacteria: carboxysomes and related microcompartments

Yeates, Todd O.; Kerfeld, Cheryl A.; Heinhorst, Sabine; Cannon, Gordon C.; Shively, Jessup

doi:10.1038/nrmicro1913

Cited by 429 publications

(413 citation statements)

References 65 publications

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“…The positive electrostatic potential of the pore has been discussed previously as a mechanism for enhancing transport of bicarbonate, but not uncharged molecules such as molecular oxygen and carbon dioxide. 6,13 Selectivity in transporting bicarbonate over CO 2 could be important in retaining CO 2 inside the carboxysome after it is generated from bicarbonate by carbonic anhydrase, thereby favoring the reaction of CO 2 with RuBisCO. In addition, or alternatively, a preference for allowing bicarbonate rather than O 2 to diffuse into the carboxysome would limit the competing, wasteful reaction of O 2 with RuBisCO.…”

Section: Discussionmentioning

confidence: 99%

“…[10][11][12] According to current models (reviewed in Ref. 13), bicarbonate from the cytosol of the bacterial cell enters the carboxysome by crossing the protein shell. Bicarbonate is then dehydrated by carbonic anhydrase to form CO 2 , which is utilized by RuBisCO before it can escape from the carboxysome.…”

Section: Introductionmentioning

confidence: 99%

“…Based on the tendency of the hexamers to pack side by side into molecular layers, it has been surmised that these layers represent the flat facets of the shell, and that the narrow pores likely serve for molecular transport. 6,7,13 A crystal structure of a BMC-type hexamer from a noncarboxysomal microcompartment-the propanediol utilization or pdu microcompartment, which requires the transport of different molecules across its shell-has a different pore structure. 25 Crystal structures of minor carboxysome shell proteins CcmL and CsoS4A, unrelated to the BMC family, were recently elucidated and found to be pentameric.…”

Section: Introductionmentioning

confidence: 99%

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Insights from multiple structures of the shell proteins from the β‐carboxysome

Sawaya²,

et al. 2008

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Carboxysomes are primitive bacterial organelles that function as a part of a carbon concentrating mechanism (CCM) under conditions where inorganic carbon is limiting. The carboxysome enhances the efficiency of cellular carbon fixation by encapsulating together carbonic anhydrase and the CO 2 -fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). The carboxysome has a roughly icosahedral shape with an outer shell between 800 and 1500 Å in diameter, which is constructed from a few thousand small protein subunits. In the cyanobacterium Synechocystis sp. PCC 6803, the previous structure determination of two homologous shell protein subunits, CcmK2 and CcmK4, elucidated how the outer shell is formed by the tight packing of CcmK hexamers into a molecular layer. Here we describe the crystal structure of the hexameric shell protein CcmK1, along with structures of mutants of both CcmK1 and CcmK2 lacking their sometimes flexible C-terminal tails. Variations in the way hexamers pack into layers are noted, while sulfate ions bound in pores through the layer provide further support for the hypothesis that the pores serve for transport of substrates and products into and out of the carboxysome. One of the new structures provides a high-resolution (1.3 Å ) framework for subsequent computational studies of molecular transport through the pores. Crystal and solution studies of the C-terminal deletion mutants demonstrate the tendency of the terminal segments to participate in proteinAprotein interactions, thereby providing a clue as to which side of the molecular layer of hexameric shell proteins is likely to face toward the carboxysome interior.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Insights from multiple structures of the shell proteins from the β‐carboxysome

Sawaya²,

et al. 2008

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“…The term microcompartment initially referred to bacterial reaction centers such as the carboxysome (Cheng et al , 2008 ;Yeates et al , 2008 ). A protein scaffold forms a rigid structure around ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase to promote carbon fixation.…”

Section: Microcompartments Within the Cytosol And Nucleusmentioning

confidence: 99%

Cellular microcompartments constitute general suborganellar functional units in cells

Holthuis

Ungermann

2013

Biological Chemistry

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All cells are compartmentalized to facilitate enzymatic reactions or cellular dynamics. In eukaryotic cells, organelles differ in their protein/lipid repertoire, luminal ion composition, pH, and redox status. In addition, organelles contain specialized subcompartments even within the same membrane or within its lumen. Moreover, the bacterial plasma membrane reveals a remarkable degree of organization, which is recapitulated in eukaryotic cells and often linked to cell signaling. Finally, protein-based compartments are also known in the bacterial and eukaryotic cytosol. As the organizing principle of such cellular subcompartments is likely similar, previous definitions like rafts, microdomains, and all kinds of ' -somes ' fall short as a general denominator to describe such suborganellar structures. Within this review, we will introduce the term cellular microcompartment as a general suborganellar functional unit and discuss its relevance to understand subcellular organization and function.

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“…The cyanobacterial CCM sequesters Rubisco into carboxysomes, which are semipermeable microcompartments surrounded by a protein shell that resembles viral capsids (9). Nearly all eukaryotic algal lineages possess a functionally analogous structure, the pyrenoid (10), which is also found in one terrestrial plant group, the ancient hornworts (11).…”

mentioning

confidence: 99%

Rubisco small-subunit α-helices control pyrenoid formation inChlamydomonas

Meyer

Genkov

Skepper

et al. 2012

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

114

118

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The pyrenoid is a subcellular microcompartment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). The pyrenoid is associated with a CO 2 -concentrating mechanism (CCM), which improves the operating efficiency of carbon assimilation and overcomes diffusive limitations in aquatic photosynthesis. Using the model alga Chlamydomonas reinhardtii, we show that pyrenoid formation, Rubisco aggregation, and CCM activity relate to discrete regions of the Rubisco small subunit (SSU). Specifically, pyrenoid occurrence was shown to be conditioned by the amino acid composition of two surface-exposed α-helices of the SSU: higher plant-like helices knock out the pyrenoid, whereas native algal helices establish a pyrenoid. We have also established that pyrenoid integrity was essential for the operation of an active CCM. With the algal CCM being functionally analogous to the terrestrial C 4 pathway in higher plants, such insights may offer a route toward transforming algal and higher plant productivity for the future.algal photosynthesis | carbon fixation | chloroplast | protein engineering

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Protein-based organelles in bacteria: carboxysomes and related microcompartments

Cited by 429 publications

References 65 publications

Insights from multiple structures of the shell proteins from the β‐carboxysome

Insights from multiple structures of the shell proteins from the β‐carboxysome

Cellular microcompartments constitute general suborganellar functional units in cells

Rubisco small-subunit α-helices control pyrenoid formation inChlamydomonas

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