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Two forms of heat-stable, zinc-containing beta-lactamase II have been described for strains of Bacillus cereus and have been shown to differ in substrate specificity (R. B. Davies, E. P. Abraham, J. Fleming, and M. R. Pollock, Biochem. J. 145: 409-411, 1975). We report here the nucleotide sequence, inferred amino acid sequence, and expression of beta-lactamase II from B. cereus 5/B/6 and compare our results with those for its homolog characterized in B. cereus 569/H (M. Hussain, C. Anthony, M. J. Madonna, and J. O. Lampen, J. Bacteriol. 164: 223-229, 1985) to document amino acid differences contributing to the specific properties of these enzymes.

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Fifty-four suppressible mutants of bacteriophage 429 have been isolated with a variety of mutagens and assigned to eight complementation groups. Viralspecific protein synthesis in UV light-irradiated, nonsuppressing Bacillus subtilis 60084 was analyzed with exponential acrylamide gels. Four additional 029 10"1 PFU of 029+ in TM buffer (0.01 M Tris-0.01 M MgSO4, pH 7.4). The mixture was incubated at room temperature (24 C) with gentle stirring. Samples (0.05 ml) were removed at 10-min intervals, and the reaction was stopped by diluting 1:100 in TMI buffer (TM containing 1 ml of a solution of 1.