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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. [ 1 ]
The Tryptophan operon leader is an RNA element found at the 5′ of some bacterial tryptophan operons. The leader sequence can form two different structures known as the terminator and the anti-terminator, based on the Tryptophan amounts in the cell. The leader also codes for very short peptide sequence that is rich in tryptophan.
The trp operon consists of a regulatory gene, a promoter, an operator, and a terminator. The trp operon is active only when cellular tryptophan is scarce. If there isn't enough tryptophan, the repressor protein breaks off from the operator (where the repressor is normally bound) and RNA polymerase can complete its reading of the strand of DNA ...
Examples include the histidine (his) [18] [19] and tryptophan (trp) [20] biosynthetic operons. The term "attenuation" was introduced to describe the his operon. [ 18 ] While it is typically used to describe biosynthesis operons of amino acids and other metabolites, programmed transcription termination that does not occur at the end of a gene ...
The total range of trp operon regulation is about 700 X (on/off). When the trp repressor was knocked out, one still got about 10 X regulation by the absence or presence of trp. When the sequence of the beginning of the trp operon was determined an unusual open reading frame (ORF) was seen immediately preceding the ORFs for the known structural ...
Organization of the trp operon in three different species of bacteria: Escherichia coli, Haemophilus influenzae, Helicobacter pylori. Only the trpA and trpB genes are adjacent across all three organisms and are thus predicted to interact by the conserved gene neighborhood method.
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The subunits of anthranilate synthase are encoded by the trpE and trpD genes in E. coli, both of which appear in the trp operon. In Enterobacteriaceae, this enzyme exists in the form of an aggregate with anthranilate phosphoribosyltransferase. If these two enzymes are not clustered, the complex is unable to use glutamine as a substrate and can ...