Modulation of gene expression in Escherichia coli infected with single-stranded bacteriophage phi X174.
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.
Ghosh
A
A
Pal
S K
SK
Poddar
R K
RK
D000469:Alkaline Phosphatase / Q000235:genetics; D010584:Bacteriophage phi X 174 / Q000235:genetics*; D000242:Cyclic AMP / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics*; D005786:Gene Expression Regulation; D012695:L-Serine Dehydratase / Q000235:genetics; D012329:RNA, Bacterial / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D012097:Repressor Proteins / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics*; D014158:Transcription, Genetic; D014368:Tryptophanase / Q000235:genetics
D012329:RNA, Bacterial; D012333:RNA, Messenger; D012097:Repressor Proteins; D014157:Transcription Factors; D000242:Cyclic AMP; D000469:Alkaline Phosphatase; D014368:Tryptophanase; D012695:L-Serine Dehydratase