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The antibiotic cerulenin differentially inhibited the production of glucosyltransferase activity by Streptococcus mutans GS5. Cerulenin preferentially inhibited [14C]acetate incorporation into cellular lipids but did not affect protein synthesis or ribonucleic acid synthesis in the same manner. No significant intracellular accumulation of glucosyltransferase activity could be demonstrated in cultures treated with cerulenin. On the other hand, another inhibitor of lipid synthesis, sodium chlorophenoxyisobutyrate, did not differentially inhibit glucosyltransferase expression. In addition, the role of a metal-requiring protease in the production of glucosyltransferase activity was suggested by the observation that the chelator quinacrine differentially inhibited the production of the enzyme.

Requirements for fatty acid synthesis and a chelation-sensitive step in the production of glucosyltransferase by Streptococcus mutans