R. Welsch et al., Regulation and activation of phytoene synthase, a key enzyme in carotenoidbiosynthesis, during photomorphogenesis, PLANTA, 211(6), 2000, pp. 846-854
During photomorphogenesis in higher plants, a coordinated increase occurs i
n the chlorophyll and carotenoid contents. The carotenoid level is tinder p
hytochrome control, as reflected by the light regulation of the mRNA level
of phytoene synthase (PSY), the first enzyme in the carotenoid biosynthetic
pathway. We investigated PSY protein levels, enzymatic activity and topolo
gical localization during photomorphogenesis. The results revealed that PSY
protein levels and enzymatic activity increase during de-etiolation and th
at the enzyme is localized at thylakoid membranes in mature chloroplasts. H
owever, under certain light conditions (e.g., far-rid light) the increases
in PSY mRNA and protein levels are not accompanied by an increase in enzyma
tic activity. Under those conditions, PSY is localized in the prolamellar b
ody fraction in a mostly enzymatically inactive form. Subsequent illuminati
on of dark-gl-own and/or in far-red light grown seedlings with white light
causes the decay of these structures and a topological relocalization of PS
Y to developing thylakoids which results in its enzymatic activation. This
light-dependent mechanism of enzymatic activation of PSY in carotenoid bios
ynthesis shares common features with the regulation of the NADPH:protochlor
ophyllide oxidoreductase, the first light-regulated enzyme in chlorophyll b
iosynthesis. The mechanism of regulation described here may contribute to e
nsuring a spatially and temporally coordinated increase in both carotenoid
and chlorophyll contents.