Effects of CO2, light and temperature on rubisco activase protein in wheat leaf segments

Herrmann, B.; Hölzer, Regina; Crafts-Brandner, Steven J.; Feller, Urs (1998). Effects of CO2, light and temperature on rubisco activase protein in wheat leaf segments. In: Garab, G (ed.) Photosynthesis: Mechanisms and Effects. Photosynthesis: Mechanisms and Effects: Vol. 3 (pp. 2059-2062). Springer

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Rubisco activase catalyzes the ATP-dependent activation of rubisco. At moderately
elevated temperature (for wheat above 30°C), rubisco activase becomes reversibly
inactivated in leaf segments (2). A further increase of the temperature (for wheat above
40°C) causes partial insolubilization and the formation of aggregates in less than 30
minutes.
Senescence in wheat leaf segments depends on the availability of CO2, the illumination
and the incubation temperature. In general, net protein degradation is delayed under
CO2 depletion. At higher light (PAR: 150 μmol m-2 s- 1), several stromal proteins are less
rapidly degraded than at low light (PAR: 50 μmol m-2 s- 1). In absence of CO2 and at the
higher PAR, chloroplast enzymes are maintained in wheat leaf segments over days even
at 35°C indicating that senescence and net degradation of chloroplast proteins are not
necessarily accelerated by such unfavorable conditions for photosynthesis. The fate of
rubisco activase protein under such conditions is of special interest, since its activity is
temperature-sensitive and this enzyme plays an important role in the regulation of
rubisco activity and as a consequence of the Calvin-cycle.

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