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J. Biol. Chem., Vol. 266, Issue 19, 12356-12360, 07, 1991
Y Ohya, M Goebl, LE Goodman, S Petersen-Bjorn, JD Friesen, F Tamanoi and Y Anraku
A 2.3-kilobase pair DNA fragment of the yeast CAL1 gene was cloned by
complementation of the cal1-1 mutation, which causes a defect in nuclear
division and bud formation (Ohya, Y., Ohsumi, Y., and Anraku, Y. (1984)
Mol. & Gen. Genet. 193, 389-394). Nucleotide sequencing of this
fragment revealed a single open reading frame (ORF) encoding a polypeptide
of 376 amino acids. Comparative analysis of the predicted amino acid
sequence has shown that the CAL1 product has similarity to two yeast
proteins: the DPR1 (RAM) gene product that is involved in processing of ras
protein at the farnesylation step, and the essential ORF2 protein whose
structural gene has a head-to-head arrangement with PRP4, which is involved
in mRNA processing. Functional homology between CAL1 and DPR1 has also been
suggested from genetic evidence that multiple copies of the CAL1 gene
suppress the growth defects of a dpr1 null mutant at high temperature. This
suppression is Ca(2+)-dependent, since it was not observed in complete
medium containing 200 microM CaCl2 but was apparent in medium containing
100 mM CaCl2. From sequence analysis of the cal1-1 mutation, together with
the alignment of the three gene products, we have concluded that the
conserved Gly328 in the C terminus is important for activity. We suggest
that the CAL1 protein participates in a ras-like C-terminal modification of
proteins involved in nuclear division and bud growth.
Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene involved in ras processing
Department of Biology, Faculty of Science, University of Tokyo, Japan.
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