Accumulation of repressor for ornithine transcarbamylase synthesis in Escherichia coli mediated by chloramphenicol

Bowne, S. W.; Rogers, Palmer

doi:10.1016/0926-6550(63)90085-9

Cited by 12 publications

(1 citation statement)

References 17 publications

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“…5, 6, 7). However, similar results have already been reported, for example, the preferential inhibition of P-galactosidase synthesis in Escherichia coli by chloramphenicol (Sypherd & Strauss, 1963) and puromycin (Sells, 1965) and of ornithine transcarbamylase synthesis by chloramphenicol (Browne & Rogers, 1963).…”

Section: Discussionsupporting

confidence: 65%

Biosynthesis of the Antibiotic Nisin by Whole Streptococcus lactis Organisms

Hurst

1966

Journal of General Microbiology

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SUMMARYA reaction mixture is described consisting of a buffered solution of amino acids, salts, growth factors and glucose in which freshly harvested washed Streptococcus Zactis incorporated radioactive tracers and synthesized nisin. Rapid nisin synthesis started after a delay of 30-60 min. but bacteria pre-incubated in the reaction mixture synthesized nisin without delay although the rate of protein synthesis remained the same as that of freshly harvested bacteria. Although growing S . Zactis is sensitive to penicillin and mitomycin these antibiotics had no effect on nisin synthesis by washed organisms. Actinomycin D inhibited uptake of tritiated uridine immediately and inhibited nisin synthesis after a delay of about 60 min. Antibiotics which interfere with protein synthesis, e.g. chloramphenicol, puromycin and terramycin also interfered with nisin synthesis. The inhibition was immediate and occurred irrespective of whether the antibiotics were added a t the beginning of an experiment or after 50 min. Nisin synthesis was more sensitive than protein synthesis. The data suggest that nisin synthesis occurs by a mechanism similar to that of protein synthesis.

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Section: Discussionsupporting

confidence: 65%

Biosynthesis of the Antibiotic Nisin by Whole Streptococcus lactis Organisms

Hurst

1966

Journal of General Microbiology

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Changes in patterns of nucleic acid and protein synthesis caused by a purine analogue

Chantrenne

1964

J. Cell. Comp. Physiol.

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A large part of the RNA made in presence of azaguanine is in a state of constant turnover. This RNA resembles pulse-labeled RNA by its chromatographic properties as well. Polyribosomes do not form or they are very labile, indicating improper interaction between ribosomes and messenger RNA. The synthesis of enzymes, e.g., catalase and penicillinase, is completely inhibited under conditions which allow some polypeptide synthesis. This is not due to long-lived messenger. No abnormal or modified pencillinase could be detected. During restoration by guanosine after azaguanine inhibition the different proteins are not made at the same pace. This may be due to a selective repression caused by accumulated abnormal RNA's. EARLY EFFECTS ON PROTEIN SYNTHESIS

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Mechanisms of bacterial resistance to antibiotics

Pitton

1972

Ergebnisse Der Physiologie Reviews of Physiology, Volume 65

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Accumulation of repressor for ornithine transcarbamylase synthesis in Escherichia coli mediated by chloramphenicol

Cited by 12 publications

References 17 publications

Biosynthesis of the Antibiotic Nisin by Whole Streptococcus lactis Organisms

Biosynthesis of the Antibiotic Nisin by Whole Streptococcus lactis Organisms

Changes in patterns of nucleic acid and protein synthesis caused by a purine analogue

Mechanisms of bacterial resistance to antibiotics

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