caa a22 4500 445889489 CHVBK 20180317145611.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s11120-011-9656-y doi (NATIONALLICENCE)springer-10.1007/s11120-011-9656-y Carboxysomes: cyanobacterial RubisCO comes in small packages [Elektronische Daten] [George Espie, Matthew Kimber] Cyanobacteria (as well as many chemoautotrophs) actively pump inorganic carbon (in the form of HCO3 −) into the cytosol in order to enhance the overall efficiency of carbon fixation. The success of this approach is dependent upon the presence of carboxysomes—large, polyhedral, cytosolic bodies which sequester ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) and carbonic anhydrase. Carboxysomes seem to function by allowing ready passage of HCO3 − into the body, but hindering the escape of evolved CO2, promoting the accumulation of CO2 in the vicinity of RubisCO and, consequently, efficient carbon fixation. This selectivity is mediated by a thin shell of protein, which envelops the carboxysome's enzymatic core and uses narrow pores to control the passage of small molecules. In this review, we summarize recent advances in understanding the organization and functioning of these intriguing, and ecologically very important molecular machines. Springer Science+Business Media B.V., 2011 Carboxysome nationallicence Cyanobacteria nationallicence Carbon concentrating mechanism nationallicence Carbonic anhydrase nationallicence RubisCO nationallicence RubisCO : Ribulose 1,5-bisphosphate carboxylase/oxygenase nationallicence CA : Carbonic anhydrase nationallicence CCM : Carbon concentrating mechanism nationallicence hcr : High CO2 requiring nationallicence eut : Ethanolamine utilization nationallicence GFP : Green fluorescent protein nationallicence RuBP : Ribulose 1,5-bisphosphate nationallicence 3PGA : 3-Phosphoglycerate nationallicence BMC : Bacterial microcompartment nationallicence PDB : Protein data bank nationallicence rmsd : Root mean square deviation nationallicence Espie George Department of Cell and Systems Biology, University of Toronto, L5L1C6, Mississauga, ON, Canada aut Kimber Matthew Department of Molecular and Cellular Biology, University of Guelph, N1G2W1, Guelph, ON, Canada aut Photosynthesis Research Springer Netherlands 109/1-3(2011-09-01), 7-20 0166-8595 109:1-3<7 2011 109 11120 https://doi.org/10.1007/s11120-011-9656-y text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11120-011-9656-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Espie George Department of Cell and Systems Biology, University of Toronto, L5L1C6, Mississauga, ON, Canada aut NATIONALLICENCE 700 1- Kimber Matthew Department of Molecular and Cellular Biology, University of Guelph, N1G2W1, Guelph, ON, Canada aut NATIONALLICENCE 773 0- Photosynthesis Research Springer Netherlands 109/1-3(2011-09-01), 7-20 0166-8595 109:1-3<7 2011 109 11120 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer