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All resonances observed in the 13C NMR spectrum of the antitumor antibiotic pactamycin and its degradation product pactamyçate have been assigned, employing off-resonance and specific proton decoupling as well as comparison with the 13C NMR spectra of the model compounds m-aminoacetophenone and ethyl 6-methylsalicylate.
By examination of the virus-specific polypeptides formed after the addition of pactamycin, an inhibitor of protein chain initiation, to infected cells, it has been possible to tentatively locate the virus coat proteins at the amino terminus of the large, virus-specific protein precursor, and, therefore, to assign the coat protein cistron to the 5' end of the RNA.
We have studied the effect of the drug pactamycin on protein synthesis in poliovirus-infected HeLa cells. At a concentration which primarily inhibits initiation of protein synthesis, the spectrum of poliovirus proteins synthesized is markedly changed. The amount of NCVP 1, the capsid precursor, is greatly reduced relative to NCVP 2 and the amount of NCVP X is slightly reduced. Since it is believed that there is only one major site for the initiation of protein synthesis on the poliovirus genome, we interpret this differential effect on the poliovirus proteins to be an indication of their relative distance from the initiation site. On this basis, we propose a gene order for the poliovirus genome (5' --> 3') of NCVP 1, NCVP X, NCVP 2.
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Two antibiotics were isolated from culture broths of a Streptomyces sp. and identified as 8"-hydroxypactamycin and 7-deoxypactamycin. The latter antibiotic was shown to be identical to cranomycin. An additional compound, 8"-hydroxypactamycate, was also isolated.
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