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PLANT PHYSIOLOGY , Vol 103, Issue 3 835-843, Copyright © 1993 by American Society of Plant Biologists
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ENVIRONMENTAL AND STRESS PHYSIOLOGY |
Photoinhibition and D1 Protein Degradation in Peas Acclimated to Different Growth Irradiances
E. M. Aro, S. McCaffery and J. M. Anderson
Commonwealth Scientific and Industrial Research Organization, Divison of Plant Industry and Cooperative Research Centre for Plant Science, G.P.O. Box 1600, Canberra, Australian Capital Territory 2601, Australia
The relationship between the susceptibility of photosystem II (PSII) to
photoinhibition in vivo and the rate of degradation of the D1 protein of
the PSII reaction center heterodimer was investigated in leaves from pea
plants (Pisum sativum L. cv Greenfeast) grown under widely contrasting
irradiances. There was an inverse linear relationship between the extent of
photoinhibition and chlorophyll (Chl) a/b ratios, with low-light leaves
being more susceptible to high light. In the presence of the
chloroplast-encoded protein synthesis inhibitor lincomycin, the
differential sensitivity of the various light-acclimated pea leaves to
photoinhibition was largely removed, demonstrating the importance of D1
protein turnover as the most crucial mechanism to protect against
photoinhibition. In the differently light-acclimated pea leaves, the rate
of D1 protein degradation (measured from [35S]methionine pulse-chase
experiments) increased with increasing incident light intensities only if
the light was not high enough to cause photoinhibition in vivo. Under
moderate illumination, the rate constant for D1 protein degradation
corresponded to the rate constant for photoinhibition in the presence of
lincomycin, demonstrating a balance between photodamage to D1 protein and
subsequent recovery, via D1 protein degradation, de novo synthesis of
precursor D1 protein, and reassembly of functional PSII. In marked
contrast, in light sufficiently high to cause photoinhibition in vivo, the
rate of D1 protein degradation no longer increased concomitantly with
increasing photoinhibition, suggesting that the rate of D1 protein
degradation is playing a regulatory role. The extent of thylakoid stacking,
indicated by the Chl a/b ratios of the differently light-acclimated pea
leaves, was linearly related to the half-life of the D1 protein in strong
light. We conclude that photoinhibition in vivo occurs under conditions in
which the rate of D1 protein degradation can no longer be enhanced to
rapidly remove irreversibly damaged D1 protein. We suggest that low-light
pea leaves, with more stacked membranes and less stroma-exposed thylakoids,
are more susceptible to photoinhibition in vivo mainly due to their slower
rate of D1 protein degradation under sustained high light and their slower
repair cycle of the photodamaged PSII centers.
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