Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes
Bräutigam A, Hofmann-Benning S, Weber APM (2008)
Plant Physiology 148(1): 568-579.
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| Veröffentlicht | Englisch
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Bräutigam, AndreaUniBi ;
Hofmann-Benning, Susanne;
Weber, Andreas P. M.
Einrichtung
Abstract / Bemerkung
C(4) plants have up to 10-fold higher apparent CO(2) assimilation rates than the most productive C(3) plants. This requires higher fluxes of metabolic intermediates across the chloroplast envelope membranes of C(4) plants in comparison with those of C(3) plants. In particular, the fluxes of metabolites involved in the biochemical inorganic carbon pump of C(4) plants, such as malate, pyruvate, oxaloacetate, and phosphoenolpyruvate, must be considerably higher in C(4) plants because they exceed the apparent rate of photosynthetic CO(2) assimilation, whereas they represent relatively minor fluxes in C(3) plants. While the enzymatic steps involved in the C(4) biochemical inorganic carbon pump have been studied in much detail, little is known about the metabolite transporters in the envelope membranes of C(4) chloroplasts. In this study, we used comparative proteomics of chloroplast envelope membranes from the C(3) plant pea (Pisum sativum) and mesophyll cell chloroplast envelopes from the C(4) plant maize (Zea mays) to analyze the adaptation of the mesophyll cell chloroplast envelope proteome to the requirements of C(4) photosynthesis. We show that C(3)- and C(4)- type chloroplasts have qualitatively similar but quantitatively very different chloroplast envelope membrane proteomes. In particular, translocators involved in the transport of triosephosphate and phosphoenolpyruvate as well as two outer envelope porins are much more abundant in C(4) plants. Several putative transport proteins have been identified that are highly abundant in C(4) plants but relatively minor in C(3) envelopes. These represent prime candidates for the transport of C(4) photosynthetic intermediates, such as pyruvate, oxaloacetate, and malate.
Erscheinungsjahr
2008
Zeitschriftentitel
Plant Physiology
Band
148
Ausgabe
1
Seite(n)
568-579
ISSN
0032-0889
Page URI
https://pub.uni-bielefeld.de/record/2915168
Zitieren
Bräutigam A, Hofmann-Benning S, Weber APM. Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes. Plant Physiology. 2008;148(1):568-579.
Bräutigam, A., Hofmann-Benning, S., & Weber, A. P. M. (2008). Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes. Plant Physiology, 148(1), 568-579. doi:10.1104/pp.108.121012
Bräutigam, Andrea, Hofmann-Benning, Susanne, and Weber, Andreas P. M. 2008. “Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes”. Plant Physiology 148 (1): 568-579.
Bräutigam, A., Hofmann-Benning, S., and Weber, A. P. M. (2008). Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes. Plant Physiology 148, 568-579.
Bräutigam, A., Hofmann-Benning, S., & Weber, A.P.M., 2008. Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes. Plant Physiology, 148(1), p 568-579.
A. Bräutigam, S. Hofmann-Benning, and A.P.M. Weber, “Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes”, Plant Physiology, vol. 148, 2008, pp. 568-579.
Bräutigam, A., Hofmann-Benning, S., Weber, A.P.M.: Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes. Plant Physiology. 148, 568-579 (2008).
Bräutigam, Andrea, Hofmann-Benning, Susanne, and Weber, Andreas P. M. “Comparative proteomics of chloroplast envelopes from C(3) and C(4) plants reveals specific adaptations of the plastid envelope to C(4) photosynthesis and candidate proteins required for maintaining C(4) metabolite fluxes”. Plant Physiology 148.1 (2008): 568-579.
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Solymosi K, Schoefs B., Photosynth Res 105(2), 2010
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Christin PA, Freckleton RP, Osborne CP., Trends Ecol Evol 25(7), 2010
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Hashiguchi A, Ahsan N, Komatsu S., Food Res Int 43(7), 2010
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Pudelski B, Kraus S, Soll J, Philippar K., Plant Biol (Stuttg) 12 Suppl 1(), 2010
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Cell-type-specific differentiation of chloroplasts in C4 plants.
Majeran W, van Wijk KJ., Trends Plant Sci 14(2), 2009
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Ludewig U, Dynowski M., Cell Mol Life Sci 66(19), 2009
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Proteomic analysis of the proplastid envelope membrane provides novel insights into small molecule and protein transport across proplastid membranes.
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Arabidopsis Tic62 and ferredoxin-NADP(H) oxidoreductase form light-regulated complexes that are integrated into the chloroplast redox poise.
Benz JP, Stengel A, Lintala M, Lee YH, Weber A, Philippar K, Gügel IL, Kaieda S, Ikegami T, Mulo P, Soll J, Bölter B., Plant Cell 21(12), 2009
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Huber SC, Edwards GE., Biochim. Biophys. Acta 462(3), 1977
PMID: 23151
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Huber SC, Edwards GE., Biochim. Biophys. Acta 462(3), 1977
PMID: 23150
Huber SC, Edwards GE., Biochim. Biophys. Acta 462(3), 1977
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Slack CR, Hatch MD, Goodchild DJ., Biochem. J. 114(3), 1969
PMID: 4309527
The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells.
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Weber A, Menzlaff E, Arbinger B, Gutensohn M, Eckerskorn C, Flugge UI., Biochemistry 34(8), 1995
PMID: 7873543
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Shevchenko A, Wilm M, Vorm O, Mann M., Anal. Chem. 68(5), 1996
PMID: 8779443
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