Differential responses to different light spectral ranges of violaxanthin de-epoxidation and accumulation of Cbr, an algal homologue of plant early light inducible proteins, in two strains of Dunaliella
G. Banet et al., Differential responses to different light spectral ranges of violaxanthin de-epoxidation and accumulation of Cbr, an algal homologue of plant early light inducible proteins, in two strains of Dunaliella, PL PHYS BIO, 37(11), 1999, pp. 875-879
Unicellular green algae of the genus Dunaliella, similar to higher plants,
respond to light stress by enhanced de-epoxidation of violaxanthin and accu
mulation of Cbr, a protein homologous to early light inducible proteins (El
ips) in plants. These proteins belong to the superfamily of chlorophyll a/b
binding proteins. Two Dunaliella strains, D. bardawil and D. salina, were
compared for these two responses under light in the UVA, blue, green and re
d spectral ranges. In D. bardawil, the two stress responses were similarly
induced under UVA, blue or red light and to a lesser extent under green lig
ht. In D. salina, a similar spectral range dependence was exhibited for vio
laxanthin de-epoxidation. However, Cbr accumulated only under UVA or blue l
ight but not under green or red light. A strong synergistic effect of a low
dose of blue light superimposed on red light resulted in Cbr accumulation.
These results reveal strain-specific differences in spectral range require
ments of the two light-stress responses. In the two strains, violaxanthin d
e-epoxidation is triggered under photosynthetically-active spectral ranges
but at least in D. salina, Cbr accumulation appears to require a specific l
ight signal additionally to a signal(s) generated by light stress. (C) Edit
ions scientifiques et medicales Elsevier SAS.