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Rubp Carboxylase in Carboxysomes of Blue Green Algae Institute

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Article / Publication Details

First-Page Preview

Abstract of Cytoplasmic Protein Microcompartmental Machines for Metabolic Interconversions

Published online: August 05, 2013
Issue release date: August 2013

Number of Print Pages: 8
Number of Figures: 3
Number of Tables: 1

ISSN: 2673-1665 (Print)
eISSN: 2673-1673 (Online)

For additional information: https://www.karger.com/MIP

Abstract

Carboxysomes are extraordinarily efficient proteinaceous microcompartments that encapsulate the primary CO2-fixing enzyme (ribulose-1,5-bisphosphate carboxylase/oxygenase, RuBisCO) in cyanobacteria and some proteobacteria. These microbodies form part of a CO2-concentrating mechanism (CCM), operating together with active CO2 and HCO3 - uptake transporters which accumulate HCO3 - in the cytoplasm of the cell. Cyanobacteria (also known as blue-green algae) are highly productive on a global scale, especially those species from open-ocean niches, which collectively contribute nearly 30% of global net primary fixation. This productivity would not be possible without a CCM which is dependent on carboxysomes. Two evolutionarily distinct forms of carboxysome are evident that encapsulate proteobacterial RuBisCO form-1A or higher-plant RuBisCO form- 1B, respectively. Based partly on RuBisCO phylogeny, the two carboxysome types are known either as α-carboxysomes, found in predominantly oceanic cyanobacteria (α-cyanobacteria) and some proteobacteria, or as β-carboxysomes, found mainly in freshwater/estuarine cyanobacteria (β-cyanobacteria). Both carboxysome types are believed to have evolved in parallel as a consequence of fluctuating atmospheric CO2 levels and evolutionary pressure acting via the poor enzymatic kinetics of RuBisCO. The three-dimensional structures and protein components of each carboxysome type reflect distinct evolutionarily strategies to the same major functions: subcellular compartmentalization and RuBisCO encapsulation, oxygen exclusion, and CO2 concentration and fixation.

© 2013 S. Karger AG, Basel

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Article / Publication Details

First-Page Preview

Abstract of Cytoplasmic Protein Microcompartmental Machines for Metabolic Interconversions

Published online: August 05, 2013
Issue release date: August 2013

Number of Print Pages: 8
Number of Figures: 3
Number of Tables: 1

ISSN: 2673-1665 (Print)
eISSN: 2673-1673 (Online)

For additional information: https://www.karger.com/MIP

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Source: https://www.karger.com/Article/Fulltext/351342

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