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THE PLANT CELL, Vol 8, Issue 12 2381-2394, Copyright © 1996 by American Society of Plant Biologists
Protein Farnesyltransferase in Plants: Molecular Characterization and Involvement in Cell Cycle Control
D. Qian, D. Zhou, R. Ju, C. L. Cramer and Z. Yang
Department of Plant Biology and Plant Molecular Biology and Biotechnology Program, Ohio State University Columbus, Ohio 43210
Farnesylation is required for membrane targeting, protein-protein
interactions, and the biological activity of key regulatory proteins, such
as Ras small GTPases and protein kinases in a wide range of eukaryotes. In
this report, we describe the molecular identification of a plant protein
farnesyltransferase (FTase) and evidence for its role in the control of the
cell cycle in plants. A pea gene encoding a homolog of the FTase [beta]
subunit was previously cloned using a polymerase chain reaction-based
strategy. A similar approach was used to clone a pea gene encoding a
homolog of the FTase [alpha] subunit. The biochemical function of the pea
FTase homologs was demonstrated by the reconstitution of FTase enzyme
activity using FTase fusion proteins coexpressed in Escherichia coli. RNA
gel blot analyses showed that levels of FTase mRNAs are generally higher in
tissues, such as those of nodules, that are active in cell division. The
relationship of FTase to cell division was further analyzed during the
growth of suspension-cultured tobacco BY-2 cells. A biphasic fluctuation of
FTase enzyme activity preceded corresponding changes in mitotic activity at
the early log phase of cell growth. Moreover, manumycin, a specific
inhibitor of FTase, was effective in inhibiting mitosis and growth in these
cells. Using synchronized BY-2 cells, manumycin completely blocked mitosis
when added at the early S phase but not when added at the G2 phase. These
data suggest that FTase is required for the plant cell cycle, perhaps by
modulating the progression through the S phase and the transition from G1
to the S phase.
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