Microcompartments in Prokaryotes: Carboxysomes and Related Polyhedra

Cannon, Gordon C.; Bradburne, Christopher; Aldrich, Henry C.; Baker, Stefanie H.; Heinhorst, Sabine; Shively, Jessup

doi:10.1128/aem.67.12.5351-5361.2001

Cited by 211 publications

(207 citation statements)

References 78 publications

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“…In cyanobacteria, the operation of a CCM generally involves a suite of CO 2 and HCO 3 -acquisition systems, as well as a distinct assembly of RubisCO and carbonic anhydrase (CA) within so-called carboxysomes (Badger and Price 2003;Cannon et al 2001;Price et al 2008;Raven 2003). Characterization of cyanobacterial C i uptake has thus far revealed five different systems, primarily based on studies with cyanobacterial strains such as Synechococcus spp.…”

Section: Inorganic Carbon Acquisitionmentioning

confidence: 99%

“…The energetic demand of the different C acquisition systems is, however, still under debate Photosynth Res differentiating the genera of cyanobacteria into two classes, the a-and b-cyanobacteria. Further information on the role of carboxysomes in the cyanobacterial CCM can be found in several reviews (Badger et al 2006;Cannon et al 2001;Kaplan and Reinhold 1999;Price et al 2002). All in all, a large diversity in CCMs has evolved that allows cyanobacteria to grow over a wide range of C i concentrations.…”

Section: Inorganic Carbon Acquisitionmentioning

confidence: 99%

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Interactions between CCM and N2 fixation in Trichodesmium

2010

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In view of the current increase in atmospheric pCO 2 and concomitant changes in the marine environment, it is crucial to assess, understand, and predict future responses of ecologically relevant phytoplankton species. The diazotrophic cyanobacterium Trichodesmium erythraeum was found to respond strongly to elevated pCO 2 by increasing growth, production rates, and N 2 fixation. The magnitude of these CO 2 effects exceeds those previously seen in other phytoplankton, raising the question about the underlying mechanisms. Here, we review recent publications on metabolic pathways of Trichodesmium from a gene transcription level to the protein activities and energy fluxes. Diurnal patterns of nitrogenase activity change markedly with CO 2 availability, causing higher diel N 2 fixation rates under elevated pCO 2 . The observed responses to elevated pCO 2 could not be attributed to enhanced energy generation via gross photosynthesis, although there are indications for CO 2 -dependent changes in ATP/ NADPH ? H ? production. The CO 2 concentrating mechanism (CCM) in Trichodesmium is primarily based on HCO 3 -uptake. Although only little CO 2 uptake was detected, the NDH complex seems to play a crucial role in internal cycling of inorganic carbon, especially under elevated pCO 2 . Affinities for inorganic carbon change over the day, closely following the pattern in N 2 fixation, and generally decrease with increasing pCO 2 . This down-regulation of CCM activity and the simultaneously enhanced N 2 fixation point to a shift in energy allocation from carbon acquisition to N 2 fixation under elevated pCO 2 levels. A strong light modulation of CO 2 effects further corroborates the role of energy fluxes as a key to understand the responses of Trichodesmium.

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Section: Inorganic Carbon Acquisitionmentioning

confidence: 99%

Section: Inorganic Carbon Acquisitionmentioning

confidence: 99%

Interactions between CCM and N2 fixation in Trichodesmium

2010

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“…The vitamin B 12 coenzymes adenosyl-B 12 (Ado-B 12 ) and methyl-B 12 ) are required cofactors for at least 15 different enzymes (5,27,30). These enzymes have a broad but uneven distribution among living forms and are vital to human health, are essential to the carbon cycle, and have important industrial applications (5,27,30).…”

mentioning

confidence: 99%

“…These enzymes have a broad but uneven distribution among living forms and are vital to human health, are essential to the carbon cycle, and have important industrial applications (5,27,30). Historically, bacteria have provided excellent model systems for the study of vitamins, and recent investigations with several bacterial systems have found the molecular biology of B 12 -dependent processes to be unexpectedly complex (9,27,29,34,35). One of the most surprising findings in this area has been the identification of a polyhedral organelle involved in coenzyme B 12 -dependent 1,2-propanediol (1,2-PD) degradation by Salmonella enterica (9).…”

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Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

2003

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Salmonella enterica forms polyhedral organelles during coenzyme B 12 -dependent growth on 1,2-propanediol (1,2-PD). Previously, these organelles were shown to consist of a protein shell partly composed of the PduA protein, the majority of the cell's B 12 -dependent diol dehydratase, and additional unidentified proteins. In this report, the polyhedral organelles involved in B 12 -dependent 1,2-PD degradation by S. enterica were purified by a combination of detergent extraction and differential and density gradient centrifugation. The course of the purification was monitored by electron microscopy and gel electrophoresis, as well as enzymatic assay of B 12 -dependent diol dehydratase. Following one-and two-dimensional gel electrophoresis of purified organelles, the identities and relative abundance of their constituent proteins were determined by N-terminal sequencing, protein mass fingerprinting, Western blotting, and densitometry. These analyses indicated that the organelles consisted of at least 15 proteins, including PduABB CDEGHJKOPTU and one unidentified protein. Seven of the proteins identified (PduABB JKTU) have some sequence similarity to the shell proteins of carboxysomes (a polyhedral organelle involved in autotrophic CO 2 fixation), suggesting that the S. enterica organelles and carboxysomes have a related multiprotein shell. In addition, S. enterica organelles contained four enzymes: B 12 -dependent diol dehydratase, its putative reactivating factor, aldehyde dehydrogenase, and ATP cob(I) alamin adenosyltransferase. This complement of enzymes indicates that the primary catalytic function of the S. enterica organelles is the conversion of 1,2-PD to propionyl coenzyme A (which is consistent with our prior proposal that the S. enterica organelles function to minimize aldehyde toxicity during growth on 1,2-PD). The possibility that similar protein-bound organelles may be more widespread in nature than currently recognized is discussed.The vitamin B 12 coenzymes adenosyl-B 12 (Ado-B 12 ) and methyl-B 12 (CH 3 -B 12 ) are required cofactors for at least 15 different enzymes (5, 27, 30). These enzymes have a broad but uneven distribution among living forms and are vital to human health, are essential to the carbon cycle, and have important industrial applications (5, 27, 30). Historically, bacteria have provided excellent model systems for the study of vitamins, and recent investigations with several bacterial systems have found the molecular biology of B 12 -dependent processes to be unexpectedly complex (9,27,29,34,35). One of the most surprising findings in this area has been the identification of a polyhedral organelle involved in coenzyme B 12 -dependent 1,2-propanediol (1,2-PD) degradation by Salmonella enterica (9).Salmonella enterica utilizes 1,2-PD as a carbon and energy source in an Ado-B 12 -dependent fashion (19). Degradation occurs aerobically, or anaerobically if tetrathionate is added as a terminal electron acceptor (26). Based on biochemical studies, a pathway for 1,2-PD degradation has been ...

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Synthetic Biology in Metabolic Engineering: From Complex Biochemical Pathways to Compartmentalized Metabolic Processes - a Vitamin Connection

Deery

Frank

Lawrence

et al. 2014

Encyclopedia of Molecular Cell Biology and Molecular Medicine

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Microcompartments in Prokaryotes: Carboxysomes and Related Polyhedra

Cited by 211 publications

References 78 publications

Interactions between CCM and N2 fixation in Trichodesmium

Interactions between CCM and N2 fixation in Trichodesmium

Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

Synthetic Biology in Metabolic Engineering: From Complex Biochemical Pathways to Compartmentalized Metabolic Processes - a Vitamin Connection

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Microcompartments in Prokaryotes: Carboxysomes and Related Polyhedra

Cited by 211 publications

References 78 publications

Interactions between CCM and N2 fixation in Trichodesmium

Interactions between CCM and N2 fixation in Trichodesmium

Protein Content of Polyhedral Organelles Involved in Coenzyme B 12 -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

Synthetic Biology in Metabolic Engineering: From Complex Biochemical Pathways to Compartmentalized Metabolic Processes - a Vitamin Connection

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Protein Content of Polyhedral Organelles Involved in Coenzyme B ₁₂ -Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2