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Vol. 8, Issue 12, 2519-2537, December 1997
Department of Developmental Biology, Howard Hughes Medical
Institute, Stanford University School of Medicine, Stanford, California
94305
The TOR proteins, originally identified as targets of the
immunosuppressant rapamycin, contain an ATM-like "lipid kinase" domain and are required for early G1 progression in eukaryotes. Using a
screen to identify Saccharomyces cerevisiae mutants
requiring overexpression of Tor1p for viability, we have isolated
mutations in a gene we call ROT1 (requires
overexpression of Tor1p). This gene is identical to
DNA2, encoding a helicase required for DNA replication.
As with its role in cell cycle progression, both the N-terminal and
C-terminal regions, as well as the kinase domain of Tor1p, are required
for rescue of dna2 mutants. Dna2 mutants are also rescued by Tor2p and show synthetic lethality with
tor1 deletion mutants under specific conditions.
Temperature-sensitive (Ts) dna2 mutants arrest
irreversibly at G2/M in a RAD9- and
MEC1-dependent manner, suggesting that Dna2p has a role
in S phase. Frequencies of mitotic recombination and chromosome loss
are elevated in dna2 mutants, also supporting a role for
the protein in DNA synthesis. Temperature-shift experiments indicate
that Dna2p functions during late S phase, although dna2
mutants are not deficient in bulk DNA synthesis. These data suggest
that Dna2p is not required for replication fork progression but may be
needed for a later event such as Okazaki fragment maturation.
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