Xm. Li et al., Phosphoenolpyruvate carboxylase in mistletoe leaves: Regulation of gene expression, protein content, and covalent modification, PHYSL PLANT, 112(3), 2001, pp. 343-352
Seasonal changes in the activity of phosphoenolpyruvate carboxylase (PEPCas
e, EC 4.1.1.31), a key enzyme in the interaction of carbohydrate and nitrog
en metabolism, were studied in leaves of the C-3 semiparasitic mistletoe, V
iscum album, growing on different host trees. Maximum extractable PEPCase a
ctivities were higher in leaves of mistletoes growing on Betula pendula and
Alnus glutinosa hosts compared with those on the conifers, Abies alba and
Larix decidua Independent of host, maximum extractable PEPCase activities m
ere high in spring and autumn while low in summer. Samples with higher PEPC
ase activities showed higher amounts of PEPCase protein and higher PEPCase
mRNA levels. A curvilinear correlation between leaf total nitrogen content
and the maximum extractable PEPCase activity as well as PEPCase mRNA level
suggested that nitrogen might affect the activity of PEPCase of mistletoe b
y up-regulating gene expression. In addition to extractable activity, seaso
nal changes of the PEPCase activation state, the ratio of activities result
ing from limited:non-limited assays, were found, which was correlated to th
e variation of malate content in leaves of mistletoe, ATP-dependent activat
ion of PEPCase was characterized by an increase in I-0.5(L-malate), indicat
ing that PEPCase of leaves of mistletoes is probably regulated via phosphor
ylation.