Mechanism of protection of protein synthesis against streptomycin inhibition in a producing strain.
The influence of streptomycin (SM) on protein synthesis in a SM-producing strain was investigated using polyuridylic acid-directed polyphenylalanine synthesis in cell-free extracts. Tolerance of protein synthesis to SM developed with increasing culture age of cells and could be attributed to a decrease in affinity of the ribosomes for SM and in increase in SM 6-kinase activity in cells. SM 6-phosphate produced from SM by SM 6-kinase did not bind to ribosomes and, furthermore, ribosome-bound SM was effectively released on phosphorylation with SM 6-kinase. Also a decrease in cell permeability to SM during the production phase may contribute in protecting protein synthesis from the antibiotic.
D001426:Bacterial Proteins / Q000096:biosynthesis*; D004096:Dihydrostreptomycin Sulfate / Q000378:metabolism; D010452:Peptide Biosynthesis; D010455:Peptides; D010766:Phosphorylation; D010770:Phosphotransferases / Q000032:analysis; D017853:Phosphotransferases (Alcohol Group Acceptor); D012270:Ribosomes / Q000378:metabolism; D013305:Streptomyces griseus / Q000187:drug effects / Q000378:metabolism*; D013307:Streptomycin / Q000096:biosynthesis / Q000494:pharmacology*
D001426:Bacterial Proteins; D010455:Peptides; C012001:polyphenylalanine; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022680:streptomycin 6-kinase; D004096:Dihydrostreptomycin Sulfate; D013307:Streptomycin