1887

Abstract

SUMMARY: Sulphate-limited continuous cultures of showed a proportional repression of nitrogenase activity with increasing concentrations of ammonium ion in the influent medium. A fully repressed population had a 50 % greater bacterial density than a fully derepressed one. On derepression, synthesis of nitrogenase lagged for 90 min after exhaustion of NH from the medium but was complete within one doubling time. Casamino acids did not decrease the pre-fixation lag obtained under sulphate-limited conditions in the chemostat. Longer lags were obtained when NH was exhausted under N-limited conditions. Such lags were decreased by Casamino acids, yeast extract, or -aspartate. Aspartate-N completely repressed nitrogenase under sulphate- or carbon-limited conditions but not under nitrogen limitation. In the initial stages of repression of nitrogenase synthesis by NH , apparent production of active enzyme continued for a short time in the absence of protein synthesis ; nitrogenase was then diluted out as the organisms multiplied. Repression by NH was at the level of mRNA transcription according to studies with rifampicin and chloramphenicol. ‘Coding capacity’ for nitrogenase synthesis declined with a half-life of about 4.5 min following inhibition of RNA synthesis with rifampicin. NH did not influence the decay rate but stimulated translation of such nitrogenase-specifying mRNA as had been initiated.

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1973-11-01
2022-01-21
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