ISSN:
1617-4623
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary Synthesis of tryptophanase, D-serine deaminase and alkaline phosphatase in Escherichia coli C was repressed as the result of infection with the single-stranded DNA bacteriophage ϕX174. However, the degree of repression differed, the more catabolite-sensitive the operon was, the more severe was the repression. For the catabolite-sensitive enzymes it was found that cyclic adenosine 3′5′ monophosphate (cyclic AMP or cAMP) was unable to release or reduce the phage-induced inhibition. Experiments with amber mutants of ϕX174 revealed that A*, product of cistron A, was responsible for the inhibition. The cistron A product probably acted at the level of transcription. The possible role of A* in the observed modulation of gene expression is discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00383011