J. Andersson et al., Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26:Implications for the mechanism of protective energy dissipation, PL CELL, 13(5), 2001, pp. 1193-1204
The specific roles of the chlorophyll alb binding proteins CP29 and CP26 in
light harvesting and energy dissipation within the photosynthetic apparatu
s have been investigated. Arabidopsis was transformed with antisense constr
ucts against the genes encoding the CP29 or CP26 apoprotein, which gave ris
e to several transgenic lines with remarkably low amounts of the antisense
target proteins. The decrease in the level of CP24 protein in the CP29 anti
sense lines indicates a physical interaction between these complexes. Analy
sis of chlorophyll fluorescence showed that removal of the proteins affecte
d photosystem II function, probably as a result of changes in the organizat
ion of the light-harvesting antenna. However, whole plant measurements show
ed that overall photosynthetic rates were similar to those in the wild type
. Both antisense lines were capable of the qE type of nonphotochemical fluo
rescence quenching, although there were minor changes in the capacity for q
uenching and in its induction kinetics. High-light-induced violaxanthin dee
poxidation to zeaxanthin was not affected, although the pool size of these
pigments was decreased slightly. We conclude that CP29 and CP26 are unlikel
y to be sites for nonphotochemical quenching.