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Functioning of the tonoplast in vacuolar C-storage and remobilization in crassulacean acid metabolism

Luttge, U ; Fischer-Schliebs, E ; Ratajczak, R ; Kramer, D ; Berndt, E ; Kluge, M

Journal of experimental botany, 1995-09, Vol.46 (special_issue), p.1377-1388 [Periódico revisado por pares]

OXFORD UNIVERSITY PRESS

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  • Título:
    Functioning of the tonoplast in vacuolar C-storage and remobilization in crassulacean acid metabolism
  • Autor: Luttge, U ; Fischer-Schliebs, E ; Ratajczak, R ; Kramer, D ; Berndt, E ; Kluge, M
  • Assuntos: active transport ; Adenosine triphosphatases ; Bryophyllum daigremontianum ; Crassulacean acid metabolism ; Cytoplasm ; Enzymes ; hydrogen ions ; Kalanchoe blossfeldiana ; literature reviews ; malic acid ; Mesembryanthemum crystallinum ; organic anions ; Photorespiration: Alternative Pathways: Carbon Allocation ; Plant cells ; Plant physiology ; Plants ; potassium ; proton pump ; Protons ; pyrophosphatases ; Tonoplast ; v0v1-ht-transporting atpase ; Vacuoles
  • É parte de: Journal of experimental botany, 1995-09, Vol.46 (special_issue), p.1377-1388
  • Descrição: Nocturnal fixation of CO2 and storage of carbon in the form of malic acid in vacuoles of photosynthetically active cells are key processes of crassulacean acid metabolism (CAM). A prerequisite for malate transport into the vacuole is the concerted action of primary-active H+-pumps, i.e. the tonoplast V0V1-H+-ATPase and H+-PP(i)ase, and a secondary-active carboxylate transporter. During the transition from C3-photosynthesis to CAM the H+-ATPase of the C3/CAM-intermediate plant Mesembryanthemum crystallinum undergoes particular structural changes indicating an adaptation of the enzyme to the requirements for an increased capacity of tonoplast transport systems. The role of the H+-PP(i)ase in energization of carbon transport in CAM remains unclear. While in Kalanchoe blossfeldiana cv. Tom Thumb, where CAM is induced by shortening of daylength, there is a higher expression of the H+-PP(i)ase in the CAM state as compared to the C3-state, the enzyme disappears in M. crystallinum when CAM is induced by salt stress. However, the H+-PP(i)ase could also be involved in the regulation of the H+-ATPase as shown by the PP(i)-stimulated ATP-dependent H+-transport activity found in K. daigremontiana and K. blossfeldiana cv. Tom Thumb. Although the tonoplast carboxylate transporter has not yet been identified, the kinetic parameters of the enzyme were characterized after partial purification and functional reconstitution into proteo-liposomes. While the influx of malate into the vacuole is mediated by the co-operation of different enzymes, the regulation of the passive efflux of malic acid from the tonoplast during the day may depend on biophysical membrane properties, i.e. the degree of order of the vacuolar membrane, which seems to be modulated by Ca2+.
  • Editor: OXFORD UNIVERSITY PRESS
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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