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J. Cell Biol.,
Volume 143, Number 6, December 14, 1998 1471-1484
in Proliferating Cells
Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology,
University of Massachusetts Medical School, Worcester, Massachusetts 01605
The zinc finger protein ZPR1 is present in
the cytoplasm of quiescent mammalian cells and translocates to the nucleus upon treatment with mitogens,
including epidermal growth factor (EGF). Homologues
of ZPR1 were identified in yeast and mammals. These ZPR1 proteins bind to eukaryotic translation elongation factor-1
(eEF-1). Studies of mammalian cells
demonstrated that EGF treatment induces the interaction of ZPR1 with eEF-1 and the redistribution of
both proteins to the nucleus. In the yeast Saccharomyces cerevisiae, genetic analysis demonstrated that ZPR1
is an essential gene. Deletion analysis demonstrated
that the NH2-terminal region of ZPR1 is required for
normal growth and that the COOH-terminal region
was essential for viability in S. cerevisiae. The yeast ZPR1 protein redistributes from the cytoplasm to the
nucleus in response to nutrient stimulation. Disruption
of the binding of ZPR1 to eEF-1 by mutational analysis resulted in an accumulation of cells in the G2/M
phase of cell cycle and defective growth. Reconstitution
of the ZPR1 interaction with eEF-1 restored normal growth. We conclude that ZPR1 is essential for cell viability and that its interaction with eEF-1 contributes
to normal cellular proliferation.
;
EGF;
Saccharomyces cerevisiae;
zinc finger
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