Abstract |
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 phi X174. 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 phi X174 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.
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Authors | A Ghosh, S K Pal, R K Poddar |
Journal | Molecular & general genetics : MGG
(Mol Gen Genet)
Vol. 198
Issue 2
Pg. 304-8
( 1985)
ISSN: 0026-8925 [Print] Germany |
PMID | 2580215
(Publication Type: Journal Article)
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Chemical References |
- RNA, Bacterial
- RNA, Messenger
- Repressor Proteins
- Transcription Factors
- Cyclic AMP
- Alkaline Phosphatase
- Tryptophanase
- L-Serine Dehydratase
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Topics |
- Alkaline Phosphatase
(genetics)
- Bacteriophage phi X 174
(genetics)
- Cyclic AMP
(physiology)
- Escherichia coli
(genetics)
- Gene Expression Regulation
- L-Serine Dehydratase
(genetics)
- RNA, Bacterial
(genetics)
- RNA, Messenger
(genetics)
- Repressor Proteins
(genetics)
- Transcription Factors
(genetics)
- Transcription, Genetic
- Tryptophanase
(genetics)
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