Posidonia oceanica meadows are among the most valuable coastal systems in the Mediterranean basin. They provide nursery and forage areas for many commercially important species, including juvenile mollusc, finfish, and crustaceans. In the Mediterranean Sea, P. oceanica beds have recently suffered from progressive die-offs attributed to lower light availability from elevated water turbidity. In order to understand adaptive low-light responses of this seagrass, we compared the protein expression in plants collected from turbid waters (low-light) with plants collected from pristine-clear waters (high-light). More than 2600 proteins were detected in leaves from both sites. Among them, 26 proteins were differentially expressed in low-light conditions, 12 of which were identified through MASCOT analyses. The remaining 14 proteins, did not receive significant identity scores due to a lack of genomic and proteomic information in available databases. Nevertheless, we observed a 30% down-regulation of RuBisCo large subunit in low-light acclimated leaves. Whereas, enzymes involved in carbohydrate cleavage (1-fructose-bisphosphate aldolase, nucleoside diphosphate kinase, and beta-amylase) were upregulated in low-light conditions. Electron microscopy studies also revealed substantial changes in the stroma lamellae/grana ratios in chloroplasts receiving lowlight, possibly as a mechanism for re-establishing optimal PSI/PSII ratios. Furthermore, under low-light conditions, four components of the ubiquitin/mediated proteolysis pathway (26 S proteasome regulatory, proteasome beta type 1, proteasome 7 D beta type, and proteasome alpha 7), and the perchloric acid soluble translation inhibitor protein, were upregulated. This suggests that, in P. oceanica leaves, enhanced protein turnover mediates acclimation to low-light conditions. Also, enzymes involved in defending against cellular stress (superoxide dismutase, pyridoxine, and 2-caffeic-acido-methyl transferase) were differentially expressed in low-light regime. Subsequent aquaria studies involving P. oceanica transplants maintained in low- and high-light conditions, also demonstrate RuBisCo down-regulation and proteasomes upregulation in low-light acclimated plants.
Seagrass light acclimation: 2-DE protein analysis in Posidonia leaves grown in chronic low light conditions
VANNINI, CANDIDA;MARSONI, MILENA;BRACALE, MARCELLA;
2009-01-01
Abstract
Posidonia oceanica meadows are among the most valuable coastal systems in the Mediterranean basin. They provide nursery and forage areas for many commercially important species, including juvenile mollusc, finfish, and crustaceans. In the Mediterranean Sea, P. oceanica beds have recently suffered from progressive die-offs attributed to lower light availability from elevated water turbidity. In order to understand adaptive low-light responses of this seagrass, we compared the protein expression in plants collected from turbid waters (low-light) with plants collected from pristine-clear waters (high-light). More than 2600 proteins were detected in leaves from both sites. Among them, 26 proteins were differentially expressed in low-light conditions, 12 of which were identified through MASCOT analyses. The remaining 14 proteins, did not receive significant identity scores due to a lack of genomic and proteomic information in available databases. Nevertheless, we observed a 30% down-regulation of RuBisCo large subunit in low-light acclimated leaves. Whereas, enzymes involved in carbohydrate cleavage (1-fructose-bisphosphate aldolase, nucleoside diphosphate kinase, and beta-amylase) were upregulated in low-light conditions. Electron microscopy studies also revealed substantial changes in the stroma lamellae/grana ratios in chloroplasts receiving lowlight, possibly as a mechanism for re-establishing optimal PSI/PSII ratios. Furthermore, under low-light conditions, four components of the ubiquitin/mediated proteolysis pathway (26 S proteasome regulatory, proteasome beta type 1, proteasome 7 D beta type, and proteasome alpha 7), and the perchloric acid soluble translation inhibitor protein, were upregulated. This suggests that, in P. oceanica leaves, enhanced protein turnover mediates acclimation to low-light conditions. Also, enzymes involved in defending against cellular stress (superoxide dismutase, pyridoxine, and 2-caffeic-acido-methyl transferase) were differentially expressed in low-light regime. Subsequent aquaria studies involving P. oceanica transplants maintained in low- and high-light conditions, also demonstrate RuBisCo down-regulation and proteasomes upregulation in low-light acclimated plants.File | Dimensione | Formato | |
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