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. 1984 Mar;49(3):806–812. doi: 10.1128/jvi.49.3.806-812.1984

Characterization of proteins induced by mitomycin C treatment of Bacillus subtilis.

C Mauël, D Karamata
PMCID: PMC255541  PMID: 6321765

Abstract

A total of 26 polypeptides have been resolved by gel electrophoresis of purified phage PBSX, 3 of which belong to the head and the remainder to the tail. After mitomycin C treatment, synthesis of 11 additional proteins which are not found in the assembled phage particle was demonstrated, all but 4 being under the control of the phage repressor. Existence of a prehead and of a precursor of the main capsid protein (molecular weight, 35,000) suggested phage head maturation which is accompanied by cleavage of the precursor (molecular weight, 36,500). The role of induced proteins related and unrelated to PBSX is discussed. Finally, the estimated phage genome mass of 4 X 10(7) daltons exceeded by more than four times its head capacity, which could explain the defectiveness of the phage.

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Selected References

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