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Cited by 335

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Photoinhibition and D1 Protein Degradation in Peas Acclimated to Different Growth Irradiances

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Aro, E. M., McCaffery, S., Anderson, J. M.·1993·Plant Physiology
DOI 10.1104/pp.103.3.835
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Abstract

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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Metadata

Authors
Aro, E. M., McCaffery, S., & Anderson, J. M.
Venue
Plant Physiology
Publisher
Oxford University Press (OUP)
Published
1993-11-01
Volume
103
Issue
3
Pages
835-843
ISSN
  • 0032-0889 (ISSN-L)
  • 1532-2548
DOI
10.1104/pp.103.3.835
OpenAlex
W1600738747
Cited by
335
References
24
FWCI
4.00
Type
journal article
Language
en
Open access
green

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