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Proline Suppresses Rubisco Activity in Higher Plants

Tipo de material: TextoTextoSeries ; BioChemical and Biophysical Research Communications, 252, p.428-432, 1998Trabajos contenidos:
  • Sivakumar, P
  • Sharmila, P
  • Pardha Saradhi, P
Recursos en línea: Resumen: Seedlings of Brassica juncea, Sesbania sesban, and Oryza sativa exposed to salt stress accumulated proline to levels as high as 4- to 20-fold over those of controls. Because chloroplasts are the major site for synthesis of stress induced proline accumulation, in vitro studies were conducted to see how the overaccumulation of this solute influences the activity of the major chloroplastic enzyme Ribulose 1,5-bisphosphate carboxylase (Rubisco)purified from the above plant species. Surprisingly, proline (believed to be a compatible solute)suppressed the activity of Rubisco significantly even when present at a concentration as low as 100 mM. The extent of this inhibition in Rubisco activity increased with an increase in the concentration of proline. Irrespective of the plant species from which Rubisco was purified, its activity declined by about 50
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Seedlings of Brassica juncea, Sesbania sesban, and Oryza sativa exposed to salt stress accumulated proline to levels as high as 4- to 20-fold over those of controls. Because chloroplasts are the major site for synthesis of stress induced proline accumulation, in vitro studies were conducted to see how the overaccumulation of this solute influences the activity of the major chloroplastic enzyme Ribulose 1,5-bisphosphate carboxylase (Rubisco)purified from the above plant species. Surprisingly, proline (believed to be a compatible solute)suppressed the activity of Rubisco significantly even when present at a concentration as low as 100 mM. The extent of this inhibition in Rubisco activity increased with an increase in the concentration of proline. Irrespective of the plant species from which Rubisco was purified, its activity declined by about 50

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