Rjn. Emery et al., ECOTYPIC DIFFERENCES IN RHYTHMICITY OF ETHYLENE PRODUCTION IN STELLARIA LONGIPES - THE POSSIBLE ROLES OF ACC, MACC, AND ACC OXIDASE, Canadian journal of botany, 75(7), 1997, pp. 1027-1033
The alpine tundra ecotype of Stellaria longipes is characterized by a
dwarf phenotype, whereas the prairie ecotype can be semidwarf or highl
y elongated depending on its environment. Related to their ability to
elongate, these ecotypes also show divergent abilities to produce and
respond to ethylene. The prairie ecotype produces a strong daily rhyth
m of ethylene, which is maintained even following stress events such a
s wind. The alpine ecotype exhibits a much less pronounced rhythm but
greatly increases ethylene production in response to stress. We invest
igated what differences in ethylene synthesis might be responsible for
the ability of the prairie ecotype to produce a large and regular dai
ly rhythm of ethylene production, which in the alpine ecotype is weake
r or sometimes absent. Levels of the immediate precursor to ethylene,
1-aminocyclopropane-1-carboxylate (ACC), and its major conjugate, malo
nyl ACC (MACC) showed no rhythm across the course of a day. Moreover A
CC levels remained stable during an entire growth cycle (21 days) in t
he prairie ecotype, even though ethylene is known to increase especial
ly during periods of rapid elongation. By contrast, assays of ACC oxid
ase performed in vivo and in vitro showed rhythms of activity similar
to those of ethylene production observed in the prairie ecotype. Howev
er, the levels of ethylene produced in the ACC oxidase assays were con
siderably higher than levels of ethylene normally produced by unstress
ed plants, and the rhythm of ACC oxidase activity was observed in both
ecotypes, despite the fact that alpine Stellaria longipes exhibits a
less pronounced ethylene rhythm. Thus, we concluded that although ACC
oxidase activity may partially account for rhythmic production of ethy
lene in prairie ecotypes, other controlling factors such as spatial se
paration of ACC from ACC oxidase should be investigated.