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Department of Microbiology, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra City A.C.T. Australia
Eighteen temperature-sensitive (ts) mutants of rabbitpox virus were examined for defects in synthesis of DNA and protein. Two mutants (ts-3 and ts-16) were defective in DNA synthesis (DNA-), since both incorporated significantly less than wild-type amounts of labelled thymidine into acid-precipitable material when infected cells were incubated at the restrictive temperature. Both these mutants gave only the early class of virus polypeptides when infected cell extracts were examined by SDS-polyacrylamide slab gel electrophoresis following incubation at 40 °C. Nine of the remaining sixteen DNA+ ts mutants (ts-1, ts-2, ts-6, ts-12, ts-15, ts-17, ts-31, ts-32 and ts-33) synthesized wild-type levels of most virus polypeptides at 40 °C; six DNA + ts mutants (ts-7, ts-8, ts-9, ts-11, ts-23 and ts-24) were defective in the post-translational cleavage of the polypeptides involved in membrane stabilization and particle assembly; one DNA+ ts mutant (ts-14) synthesized only the early class of virus polypeptides, implying that either replicated DNA was not fully functional or that a specific early function was required for late transcription.
* To whom reprint requests should be addressed.
Received 8 June 1979;
accepted 25 September 1979.
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