CO2 Acquisition, Concentration and Fixation in Cyanobacteria and Algae

Badger, Murray R.; Spalding, Martin H.

doi:10.1007/0-306-48137-5_16

Cited by 69 publications

(62 citation statements)

References 152 publications

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“…To prevent rapid leakage of accumulated HCO 3 Ϫ from the cytoplasm, the enzyme carbonic anhydrase (CA) must be absent from this compartment (19,20) to restrict CO 2 production (though this may not necessarily be true of some structurally complex cyanobacteria, such as Chlorogloeopsis fritschii and Anabaena variabilis, whose cells contain some cytoplasmic CA activity [21,22]). Nonetheless, the accumulated HCO 3 Ϫ needs to be converted to CO 2 and utilized by RubisCO in carboxysome microcompartments where CO 2 is elevated by localized production of CO 2 (1,2,4,14,(23)(24)(25)(26). The requirement of carboxysomes is known to be essential for proper CCM function, largely as a result of the analysis of a large number of characterized mutants in which carboxysome functionality is destroyed (see Table 2), leading to an inability to elevate CO 2 levels in the carboxysome, even though the cells are still able to hyperaccumulate HCO 3 Ϫ in the cytosol (see below).…”

Section: Evolutionary Pressures Due To Rubisco and Altered Atmospherimentioning

confidence: 99%

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria

Rae

Long

Badger

et al. 2013

Microbiol Mol Biol Rev

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368

450

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SUMMARY Cyanobacteria are the globally dominant photoautotrophic lineage. Their success is dependent on a set of adaptations collectively termed the CO 2 -concentrating mechanism (CCM). The purpose of the CCM is to support effective CO 2 fixation by enhancing the chemical conditions in the vicinity of the primary CO 2 -fixing enzyme, d -ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO), to promote the carboxylase reaction and suppress the oxygenase reaction. In cyanobacteria and some proteobacteria, this is achieved by encapsulation of RubisCO within carboxysomes, which are examples of a group of proteinaceous bodies called bacterial microcompartments. Carboxysomes encapsulate the CO 2 -fixing enzyme within the selectively permeable protein shell and simultaneously encapsulate a carbonic anhydrase enzyme for CO 2 supply from a cytoplasmic bicarbonate pool. These bodies appear to have arisen twice and undergone a process of convergent evolution. While the gross structures of all known carboxysomes are ostensibly very similar, with shared gross features such as a selectively permeable shell layer, each type of carboxysome encapsulates a phyletically distinct form of RubisCO enzyme. Furthermore, the specific proteins forming structures such as the protein shell or the inner RubisCO matrix are not identical between carboxysome types. Each type has evolutionarily distinct forms of the same proteins, as well as proteins that are entirely unrelated to one another. In light of recent developments in the study of carboxysome structure and function, we present this review to summarize the knowledge of the structure and function of both types of carboxysome. We also endeavor to cast light on differing evolutionary trajectories which may have led to the differences observed in extant carboxysomes.

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Section: Evolutionary Pressures Due To Rubisco and Altered Atmospherimentioning

confidence: 99%

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria

Rae

Long

Badger

et al. 2013

Microbiol Mol Biol Rev

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368

450

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“…PCC 6301, 2 Synechococcus sp. PCC 7002, 3 Anabaena PCC 7120 (www.kazusa.or.jp/cyano/), Nostoc punctiforme, P. marinus strains MED4 and MIT9313 (www.jgi.doe.gov/tempweb/ JGI_microbial/html/index.html) and in the non-photosynthetic bacteria Mycobacterium tuberculosis (23), Caulobacter crescentus (24), and Bacillus halodurans (25).…”

Section: Phylogenetic Analysis Of Sbta and Ntpj In Cyanobacteria-mentioning

confidence: 99%

“…1 which raises the [CO 2 ] in close proximity to ribulose-1,5-bisphosphate carboxylase/oxygenase and thereby enables efficient CO 2 fixation despite the low affinity of the enzyme for CO 2 (1,2). In the cyanobacterium Synechocystis sp.…”

mentioning

confidence: 99%

Genes Essential to Sodium-dependent Bicarbonate Transport in Cyanobacteria

Shibata¹,

Katoh²,

Sonoda³

et al. 2002

Journal of Biological Chemistry

258

220

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The cyanobacterium Synechocystis sp. strain PCC 6803 possesses two CO 2 uptake systems and two HCO 3 ؊ transporters. We transformed a mutant impaired in CO 2 uptake and in cmpA-D encoding a HCO 3 ؊ transporter with a transposon inactivation library, and we recovered mutants unable to take up HCO 3 ؊ and grow in low CO 2 at pH 9.0. They are all tagged within slr1512 (designated sbtA). We show that SbtA-mediated transport is induced by low CO 2 , requires Na ؉ , and plays the major role in HCO 3 ؊ uptake in Synechocystis. Inactivation of slr1509 (homologous to ntpJ encoding a Na ؉ /K ؉ -translocating protein) abolished the ability of cells to grow at [Na ؉ ] higher than 100 mM and severely depressed the activity of the SbtA-mediated HCO 3 ؊ transport. We propose that the SbtA-mediated HCO 3 ؊ transport is driven by ⌬Na ؉ across the plasma membrane, which is disrupted by inactivating ntpJ. Phylogenetic analyses indicated that two types of sbtA exist in various cyanobacterial strains, all of which possess ntpJ. The sbtA gene is the first one identified as essential to Na ؉ -dependent HCO 3 ؊ transport in photosynthetic organisms and may play a crucial role in carbon acquisition when CO 2 supply is limited, or in Prochlorococcus strains that do not possess CO 2 uptake systems or Cmp-dependent HCO 3 ؊ transport.Growth of many photosynthetic microorganisms depends on the activity of a CO 2 -concentrating mechanism (CCM), 1 which raises the [CO 2 ] in close proximity to ribulose-1,5-bisphosphate carboxylase/oxygenase and thereby enables efficient CO 2 fixation despite the low affinity of the enzyme for CO 2 (1, 2). In the cyanobacterium Synechocystis sp. strain PCC 6803 (hereafter Synechocystis 6803), the CCM involves active CO 2 uptake and HCO 3 Ϫ transport. We have recently identified two systems for CO 2 uptake in Synechocystis 6803, one constitutive and the other inducible by low CO 2 (3). As deduced from phylogenetic analysis of proteins encoded by the genes involved, these CO 2 uptake systems are present in various cyanobacteria with the exception of Prochlorococcus marinus (3). The inducible system that depends on NdhD3/ NdhF3/CupA shows higher maximal activity and higher affinity for CO 2 than the constitutive, NdhD4/NdhF4/CupB-dependent system. Inactivation of two different genes, one encoding a component of the constitutive system and the other a constituent of the inducible system, abolished CO 2 uptake activity. The double mutants were unable to grow at pH 7.0 under air level of CO 2 (3, 4). In contrast, because the mutants possessed HCO 3 Ϫ transport capability, they could grow like the wild type (WT) at pH 9.0 in air.An ABC-type HCO 3 Ϫ transporter encoded by cmpABCD has been identified in Synechococcus sp. strain PCC 7942 (thereafter Synechococcus 7942) (5). Inactivation of cmp genes in Synechocystis 6803, however, had little effect on the HCO 3 Ϫ transport activity. This indicated that another HCO 3 Ϫ transporter, as yet unidentified, plays a central role in HCO 3 Ϫ uptake. Sodium ions are essential for ...

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“…NDH-1 complexes with other NdhD and NdhF gene products have been suggested to have additional functions in carbon concentrating mechanisms in cyanobacteria (Ohkawa et al, 1998(Ohkawa et al, , 2000aPrice et al, 1998;Klughammer et al, 1999;Shibata et al, 2001;Maeda et al, 2002). These mechanisms are important in aquatic organisms to overcome the low affinity of their ribulose-1,5-bisphosphate carboxylase/oxygenase to CO 2 (Volokita et al, 1984;Kaplan and Reinhold, 1999;Badger and Spalding, 2000;Price et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Expression and Functional Roles of the Two Distinct NDH-1 Complexes and the Carbon Acquisition Complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp PCC 6803

et al. 2004

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To investigate the (co)expression, interaction, and membrane location of multifunctional NAD(P)H dehydrogenase type 1 (NDH-1) complexes and their involvement in carbon acquisition, cyclic photosystem I, and respiration, we grew the wild type and specific ndh gene knockout mutants of Synechocystis sp PCC 6803 under different CO 2 and pH conditions, followed by a proteome analysis of their membrane protein complexes. Typical NDH-1 complexes were represented by NDH-1L (large) and NDH-1M (medium size), located in the thylakoid membrane. The NDH-1L complex, missing from the DNdhD1/D2 mutant, was a prerequisite for photoheterotrophic growth and thus apparently involved in cellular respiration. The amount of NDH-1M and the rate of P700 þ rereduction in darkness in the DNdhD1/D2 mutant grown at low CO 2 were similar to those in the wild type, whereas in the M55 mutant (DNdhB), lacking both NDH-1L and NDH-1M, the rate of P700 þ rereduction was very slow. The NDH-1S (small) complex, localized to the thylakoid membrane and composed of only NdhD3, NdhF3, CupA, and Sll1735, was strongly induced at low CO 2 in the wild type as well as in DNdhD1/D2 and M55. In contrast with the wild type and DNdhD1/D2, which show normal CO 2 uptake, M55 is unable to take up CO 2 even when the NDH-1S complex is present. Conversely, the DNdhD3/D4 mutant, also unable to take up CO 2 , lacked NDH-1S but exhibited wild-type levels of NDH-1M at low CO 2 . These results demonstrate that both NDH-1S and NDH-1M are essential for CO 2 uptake and that NDH-1M is a functional complex. We also show that the Na þ /HCO 3 ÿ transporter (SbtA complex) is located in the plasma membrane and is strongly induced in the wild type and mutants at low CO 2 .

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CO2 Acquisition, Concentration and Fixation in Cyanobacteria and Algae

Cited by 69 publications

References 152 publications

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria

Genes Essential to Sodium-dependent Bicarbonate Transport in Cyanobacteria

Expression and Functional Roles of the Two Distinct NDH-1 Complexes and the Carbon Acquisition Complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp PCC 6803

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CO2 Acquisition, Concentration and Fixation in Cyanobacteria and Algae

Cited by 69 publications

References 152 publications

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO 2 Fixation in Cyanobacteria and Some Proteobacteria

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO 2 Fixation in Cyanobacteria and Some Proteobacteria

Genes Essential to Sodium-dependent Bicarbonate Transport in Cyanobacteria

Expression and Functional Roles of the Two Distinct NDH-1 Complexes and the Carbon Acquisition Complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp PCC 6803

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Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria

Functions, Compositions, and Evolution of the Two Types of Carboxysomes: Polyhedral Microcompartments That Facilitate CO ₂ Fixation in Cyanobacteria and Some Proteobacteria