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Vol. 9, Issue 8, 2025-2036, August 1998
§ and
*Department of Pharmacological Sciences, State University of New
York, Stony Brook, New York 11794-8651; and
§Department of
Biochemistry, Emory University, School of Medicine, Atlanta, Georgia
30322-3050
ADP-ribosylation factor (ARF) proteins in Saccharomyces
cerevisiae are encoded by two genes, ARF1 and
ARF2. The addition of the c-myc epitope at the C
terminus of Arf1 resulted in a mutant (arf1-myc arf2)
that supported vegetative growth and rescued cells from
supersensitivity to fluoride, but homozygous diploids failed to
sporulate. arf1-myc arf2 mutants completed both meiotic
divisions but were unable to form spores. The SPO14 gene
encodes a phospholipase D (PLD), whose activity is essential for
mediating the formation of the prospore membrane, a prerequisite event
for spore formation. Spo14 localized normally to the developing
prospore membrane in arf1-myc arf2 mutants; however, the
synthesis of the membrane was attenuated. This was not a consequence of
reduced PLD catalytic activity, because the enzymatic activity of Spo14
was unaffected in meiotic arf1-myc arf2 mutants.
Although potent activators of mammalian PLD1, Arf1 proteins did not
influence the catalytic activities of either Spo14 or ScPld2, a second
yeast PLD. These results demonstrate that ARF1 is
required for sporulation, and the mitotic and meiotic functions of Arf
proteins are not mediated by the activation of any known yeast PLD
activities. The implications of these results are discussed with
respect to current models of Arf signaling.
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