A Novel Evolutionary Lineage of Carbonic Anhydrase (ε Class) Is a Component of the Carboxysome Shell

So, Anthony K.-C.; Espie, George S.; Williams, Eric B.; Shively, Jessup; Heinhorst, Sabine; Cannon, Gordon C.

doi:10.1128/jb.186.3.623-630.2004

Cited by 258 publications

(246 citation statements)

References 38 publications

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“…It also suggests that CcaA is likely to be associated with the carboxysome shell. This is analogous to the findings for the ␣-carboxysomal CA (CsoS3), which has been localized to the carboxysome shell of H. neapolitanus (41,42), and partly supports a model put forward by Reinhold et al (43), which places CcaA within bundles of Rubisco.…”

Section: Rubisco Complexsupporting

confidence: 87%

Analysis of Carboxysomes from Synechococcus PCC7942 Reveals Multiple Rubisco Complexes with Carboxysomal Proteins CcmM and CcaA

Long

Badger

Whitney

et al. 2007

Journal of Biological Chemistry

173

224

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In cyanobacteria, the key enzyme for photosynthetic CO 2 fixation, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), is bound within proteinaceous polyhedral microcompartments called carboxysomes. Cyanobacteria with Form IB Rubisco produce ␤-carboxysomes whose putative shell proteins are encoded by the ccm-type genes. To date, very little is known of the protein-protein interactions that form the basis of ␤-carboxysome structure. In an effort to identify such interactions within the carboxysomes of the ␤-cyanobacterium Synechococcus sp. PCC7942, we have used polyhistidine-tagging approaches to identify at least three carboxysomal subcomplexes that contain active Rubisco. In addition to the expected L 8 S 8 Rubisco, which is the major component of carboxysomes, we have identified two Rubisco complexes containing the putative shell protein CcmM, one of which also contains the carboxysomal carbonic anhydrase, CcaA. The complex containing CcaA consists of Rubisco and the full-length 58-kDa form of CcmM (M58), whereas the other is made up of Rubisco and a short 35-kDa form of CcmM (M35), which is probably translated independently of M58 via an internal ribosomal entry site within the ccmM gene. We also show that the high CO 2 -requiring ccmM deletion mutant (⌬ccmM) can achieve nearly normal growth rates at ambient CO 2 after complementation with both wild type and chimeric (His 6 -tagged) forms of CcmM. Although a significant amount of independent L 8 S 8 Rubisco is confined to the center of the carboxysome, we speculate that the CcmMCcaA-Rubisco complex forms an important assembly coordination within the carboxysome shell. A speculative carboxysome structural model is presented.Prokaryotic organisms are distinct from their eukaryotic counterparts by the absence of specialized membrane-bound compartments. Although it is commonly considered that prokaryotic cells do not compartmentalize cellular processes, there is growing evidence that cyanobacteria and some ␤-proteobacteria have the means to do so when certain enzymes need to be sequestered or protected for maximal catalytic activity (1-3). Carboxysomes, for example, are polyhedral protein microcompartments found in cyanobacteria and chemoautotrophic bacteria, which contain the majority of a cell's ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (4). These microcompartments are essential to the operation of the CO 2 -concentrating mechanism in cyanobacteria. The CO 2 -concentrating mechanism utilizes a number of inorganic carbon (C i , the sum of CO 2 and HCO 3 Ϫ ) transport systems to elevate cellular HCO 3 Ϫ concentrations prior to CO 2 fixation (for reviews, see Refs. 5 and 6). Rubisco is a hexadecameric enzyme with a core of eight large subunits (L 8 ) made up of four L 2 dimers, each containing two catalytic sites. Attached to each end of the L 8 core are four small subunits (S 8 ) that are necessary for catalytic competence (7). Rubisco carries out the CO 2 fixation process in the initial step of the Calvin cycle, yet it is characterized by ...

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Section: Rubisco Complexsupporting

confidence: 87%

Analysis of Carboxysomes from Synechococcus PCC7942 Reveals Multiple Rubisco Complexes with Carboxysomal Proteins CcmM and CcaA

Long

Badger

Whitney

et al. 2007

Journal of Biological Chemistry

173

224

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“…According to the accepted classification, CAs are divided into three main classes, a, b and c, which have no significant primary sequence identity and, supposedly, are evolutionarily independent (Smith & Ferry, 2000). The existence of additional d and e classes of CAs have also been reported (Tripp et al, 2001;So et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Extracellular carbonic anhydrases of the stromatolite-forming cyanobacterium Microcoleus chthonoplastes

et al. 2007

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“…Sequences can be used for microarray anlysis, molecular systematics, vector construction or primer design. In addition, new and ancient metabolic pathways may be traced by means of gene sequences (Bhattacharya et al 1992;Des Marais 2000;Ferris et al 1997;Kumada et al 1993;So et al 2004). Our initial EST analysis involved the partial sequencing of 3527 cDNA clones from E. huxleyi cultures grown in phosphate limiting media, conditions known to promote biomineralization and coccolithogenesis (Wahlund et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Expressed sequence tag profiles from calcifying and non-calcifying cultures of Emiliania huxleyi

2004

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Expressed Sequence Tag (EST) analysis is a powerful means for evaluating gene expression and discovering novel genes. The method is relatively simple and particularly important for species where knowledge of the genome is unavailable or limited. In this study, we compare EST profiles of Emiliania huxleyi cultures grown under conditions that promote biomineralization and coccolithogenesis (F/50 media) and conditions that reduce these processes (F/2 media). A total of 3,527 clones from the F/50 and 4,116 clones from F/2 library were randomly selected and sequenced, resulting in a unigene set of 4,057 unique sequences comprised of 540 contigs and 3517 singletons. More than 40% of the expressed genes showed similarity to known genes from other organisms deposited in GenBank (e>10 -2 ) and have been functionally categorized. The comparative data provide cues for further studies pertaining to genes and proteins involved in biomineralization and coccolithogenesis, and taken together serve as a valuable resource for the coccolithophorid research community.

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A Novel Evolutionary Lineage of Carbonic Anhydrase (ε Class) Is a Component of the Carboxysome Shell

Cited by 258 publications

References 38 publications

Analysis of Carboxysomes from Synechococcus PCC7942 Reveals Multiple Rubisco Complexes with Carboxysomal Proteins CcmM and CcaA

Analysis of Carboxysomes from Synechococcus PCC7942 Reveals Multiple Rubisco Complexes with Carboxysomal Proteins CcmM and CcaA

Extracellular carbonic anhydrases of the stromatolite-forming cyanobacterium Microcoleus chthonoplastes

Expressed sequence tag profiles from calcifying and non-calcifying cultures of Emiliania huxleyi

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