Eighteen temperature-sensitive () mutants of rabbitpox virus were examined for defects in synthesis of DNA and protein. Two mutants (-3 and -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 mutants (-1, -2, -6, -12, -15, -17, -31, -32 and -33) synthesized wild-type levels of most virus polypeptides at 40 °C; six DNA + mutants (-7, -8, -9, -11, -23 and -24) were defective in the post-translational cleavage of the polypeptides involved in membrane stabilization and particle assembly; one DNA mutant (-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.


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