The trp operon is a group of genes that are transcribed together, encoding the enzymes that produce the amino acid tryptophan in bacteria. The trp operon was first characterized in Escherichia coli, and it has since been discovered in many other bacteria. The operon is regulated so that, when tryptophan is present in the environment, the genes for tryptophan synthesis are repressed.
The trp operon contains five structural genes: trpE, trpD, trpC, trpB, and trpA, which encode the enzymes needed to synthesize tryptophan. It also contains a repressive regulator gene called trpR. When tryptophan is present, the trpR protein binds to the operator, blocking transcription of the trp operon by RNA polymerase. This operon is an example of repressible negative regulation of gene expression. The repressor protein binds to the operator in the presence of tryptophan (repressing transcription) and is released from the operon when tryptophan is absent (allowing transcription to proceed). The trp operon additionally uses attenuation to control expression of the operon, a second negative feedback control mechanism. The trp operon is well-studied and is commonly used as an example of gene regulation in bacteria alongside the lac operon.
Genes trp operon contains five structural genes. The roles of their products are: TrpE (P00895): Anthranilate synthase produces anthranilate. TrpD (P00904): Cooperates with TrpE. TrpC (P00909): Phosphoribosylanthranilate isomerase domain first turns N-(5-phospho-β-D-ribosyl)anthranilate into 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. The Indole-3-glycerol-phosphate synthase on the same protein then turns the product into (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate. TrpA (P0A877), TrpB (P0A879): two subunits of tryptophan synthetase. Combines TrpC's product with serine to produce tryptophan.
Repression
The operon operates by a negative repressible feedback mechanism. The repressor for the trp operon is produced upstream by the trpR gene, which is constitutively expressed at a low level. Synthesized trpR monomers associate into dimers. When tryptophan is present, these tryptophan repressor dimers bind to tryptophan, causing a change in the repressor conformation, allowing the repressor to bind to the operator. This prevents RNA polymerase from binding to and transcribing the operon, so tryptophan is not produced from its precursor. When tryptophan is not present, the repressor is in its inactive conformation and cannot bind the operator region, so transcription is not inhibited by the repressor.
Attenuation
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