The localisation of 2-carboxy-D-arabinitol 1-phosphate and inhibition of Rubisco in leaves of Phaseolus vulgaris L

FEBS Lett. 1999 Feb 5;444(1):106-10. doi: 10.1016/s0014-5793(99)00038-1.

Abstract

A recent controversial report suggests that the nocturnal inhibitor of Rubisco, 2-carboxy-D-arabinitol 1-phosphate (CAIP), does not bind to Rubisco in vivo and therefore that CA1P has no physiological relevance to photosynthetic regulation. It is now proved that a direct rapid assay can be used to distinguish between Rubisco-bound and free CA1P, as postulated in the controversial report. Application of this direct assay demonstrates that CA1P is bound to Rubisco in vivo in dark-adapted leaves. Furthermore, CA1P is shown to be in the chloroplasts of mesophyll cells. Thus, CA1P does play a physiological role in the regulation of Rubisco.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Chlorophyll / analysis
  • Chloroplasts / chemistry
  • Chloroplasts / enzymology
  • Chloroplasts / metabolism
  • Enzyme Inhibitors / metabolism
  • Fabaceae / enzymology*
  • Fabaceae / metabolism
  • Freeze Drying
  • Light
  • Pentosephosphates / metabolism*
  • Photoperiod
  • Plant Leaves / enzymology
  • Plant Leaves / metabolism*
  • Plants, Medicinal*
  • Ribulose-Bisphosphate Carboxylase / antagonists & inhibitors*
  • Ribulose-Bisphosphate Carboxylase / metabolism
  • Sulfates / pharmacology
  • Time Factors

Substances

  • Enzyme Inhibitors
  • Pentosephosphates
  • Sulfates
  • 2-carboxyarabinitol 1-phosphate
  • Chlorophyll
  • Ribulose-Bisphosphate Carboxylase