Open AccessRelationship Between Exoprotease Secretion and the Synthesis of Ribonucleic Acid and Protein in Bacillus amyloliquefaciens
Author(s) -
G. Coleman,
Samuel Brown
Publication year - 1975
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.7.6.840
Subject(s) - bacillus amyloliquefaciens , bacteria , protein biosynthesis , messenger rna , rna , chloramphenicol , exoenzyme , microbiology and biotechnology , biology , uracil , bacterial growth , secretion , antibiotics , amino acid , biochemistry , chemistry , gene , dna , genetics
Studies with washed bacteria suspended in fresh medium, in which bacterial densities were altered by a factor of four so as to cause accelerated entry of exponential bacteria into the postexponential phase and to re-establish growth in postexponential bacteria, have been performed. Under all the conditions examined rifampin, at a concentration of 0.5 μg/ml, inhibited [14 C]uracil incorporation into total ribonucleic acid (RNA) by 90 to 95%. The percentage of inhibition of incorporation of14 C-labeled amino acids into total protein achieved in parallel experiments was less, being not more than 80%. These results suggested that non-translatable RNA synthesis was inhibited more than messenger RNA (mRNA) by the antibiotic. It was found that on slowing the growth of exponential-phase bacteria exoprotease was formed at a high rate without a lag. It was further observed that when postexponential bacteria were induced to grow, by resuspending them at a lower density, exoprotease mRNA synthesis was switched off. The only synthesis of exoprotease which occurred in this case was accountable to pre-existing mRNA during its decay. Exoenzyme formation was found to be less susceptible to rifampin than total protein synthesis.