Defensive strategies against high light stress in wild and D1 protein mutant biotypes of Erigeron canadensis

Citation
E. Darko et al., Defensive strategies against high light stress in wild and D1 protein mutant biotypes of Erigeron canadensis, AUST J PLAN, 27(4), 2000, pp. 325-333
Citations number
52
Categorie Soggetti
Plant Sciences","Animal & Plant Sciences
Journal title
AUSTRALIAN JOURNAL OF PLANT PHYSIOLOGY
ISSN journal
03107841 → ACNP
Volume
27
Issue
4
Year of publication
2000
Pages
325 - 333
Database
ISI
SICI code
0310-7841(2000)27:4<325:DSAHLS>2.0.ZU;2-D
Abstract
The Ser(264)-->Gly substitution on the D1 protein is accompanied by a highe r photosensitivity of the mutant plant. This may be due to an increased D1 protein turnover and/or to a lower xanthophyll cycle activity in vivo. The relative importance of these two photoprotective mechanisms in wild and D1 protein mutant biotypes of Erigeron canadensis L. was established by using dithiothreitol and streptomycin. Moreover, the interconversion of violaxant hin to zeaxanthin via antheraxanthin was studied in isolated thylakoids and in intact leaves treated with paraquat. Streptomycin caused a more severe decrease in the optimal quantum yield (F-v/F-m) of PS II and a large increa se in the initial fluorescence yield (F-o) in the mutant compared to the wi ld biotype. In the fluorescence-quenching parameters of the wild-type leave s, dithiothreitol caused alterations similar to those observed in the mutan t plant without dithiothreitol. A lowered activity of the xanthophyll cycle was detected in the mutant biotype compared to the wild-type in vivo. Howe ver, under in vitro, conditions which were optimal for violaxanthin de-epox idation, or when paraquat was used on intact leaves to accelerate the elect ron transport, violaxanthin could readily be converted to zeaxanthin even i n the mutant plants. This demonstrates that neither the decrease in the enz ymatic activity of violaxanthin de-epoxidase nor the low availability of vi olaxanthin is responsible for the low zeaxanthin formation under in vivo co nditions. It is presumed that, in vivo, the D1 protein mutation results in slower electron transport, a smaller Delta pH and lower zeaxanthin formatio n, and thereby in alterations in the defensive strategies against high ligh t illumination.