Trp operon


Trp operon

If unfamiliar with these terms, visit the operon page first.

Trp operon is an operon in bacteria which promotes the production of tryptophan when tryptophan isn't present in the environment. Discovered in 1953 by Jacques Monod and colleagues, the trp operon in "E. coli" was the first repressible operon to be discovered. While the lac operon can be activated by a chemical (allolactose), the tryptophan (Trp) operon is inhibited by a chemical (tryptophan). This operon contains five structural genes: trp E, trp D, trp C, trp B, and trp A, which encodes tryptophan synthetase. It also contains a promoter which binds to RNA polymerase and an operator which blocks transcription when bound to the protein synthesized by the repressor gene (trp R) that binds to the operator. In the lac operon, lactose binds to the repressor protein and prevents it from repressing gene transcription, while in the trp operon, tryptophan binds to the repressor protein and enables it to repress gene transcription. Also unlike the lac operon, the trp operon contains a leader peptide and an attenuator sequence which allows for graded regulation. [William Klug, Cummings, and Spencer. "Concepts of Genetics." 8th Ed. Pearson Education Inc, New Jersey: 2006. pg. 394-402]

It is an example of negative regulation of gene expression. Within the operon's regulatory sequence, the operator is blocked by the repressor protein in the presence of tryptophan (thereby preventing transcription) and is liberated in tryptophan's absence (thereby allowing transcription). The process of attenuation (explained below) complements this regulatory action.

Repression

The repressor for the trp operon is produced upstream by the trpR gene, which is continually expressed. It creates monomers, which associate into tetramers. When tryptophan is present, it binds to the tryptophan repressor tetramers, and causes a change in conformation, which allows the repressor to bind the operator, which prevents RNA polymerase from binding or transcribing the operon, so tryptophan is not produced. When tryptophan is not present, the repressor cannot bind the operator, so transcription can occur. This is therefore a negative feedback mechanism.

Attenuation

Attenuation is a second mechanism of negative feedback in the trp operon. While the TrpR repressor decreases transcription by a factor of 70, attenuation can further decrease it by a factor of 10, thus allowing accumulated repression of about 700-fold. Attenuation is made possible by the fact that in prokaryotes (which have no nucleus), the ribosomes begin translating the mRNA while RNA polymerase is still transcribing the DNA sequence. This allows the process of translation to directly affect transcription of the operon.

At the beginning of the transcribed genes of the trp operon is a sequence of 140 nucleotides termed the leader transcript (trpL). This transcript includes four short sequences designated 1-4. Sequence 1 is partially complementary to sequence 2, which is partially complementary to sequence 3, which is partially complementary to sequence 4. Thus, three distinct secondary structures (hairpins) can form: 1-2, 2-3 or 3-4. The hybridization of strands 1 and 2 to form the 1-2 structure prevents the formation of the 2-3 structure, while the formation of 2-3 prevents the formation of 3-4. The 3-4 structure is a transcription termination sequence, once it forms RNA polymerase will disassociate from the DNA and transcription of the structural genes of the operon will not occur.

Part of the leader transcript codes for a short polypeptide of 14 amino acids, termed the leader peptide. This peptide contains two adjacent tryptophan residues, which is unusual, since tryptophan is a fairly uncommon amino acid (about one in a hundred residues in a typical "E. coli" protein is tryptophan). If the ribosome attempts to translate this peptide while tryptophan levels in the cell are low, it will stall at either of the two trp codons. While it is stalled, the ribosome physically shields sequence 1 of the transcript, thus preventing it from forming the 1-2 secondary structure. Sequence 2 is then free to hybridize with sequence 3 to form the 2-3 structure, which then prevents the formation of the 3-4 termination hairpin. RNA polymerase is free to continue transcribing the entire operon.If tryptophan levels in the cell are high, the ribosome will translate the entire leader peptide without interruption and will only stall during translation termination at the stop codon. At this point the ribosome physically shields both sequences 1 and 2. Sequences 3 and 4 are thus free to form the 3-4 structure which terminates transcription. The end result is that the operon will be transcribed only when tryptophan is unavailable for the ribosome, while the trpL transcript is constitutively expressed.

To ensure that the ribosome binds and begins translation of the leader transcript immediately following its synthesis, a pause site exists in the trpL sequence. Upon reaching this site, RNA polymerase pauses transcription and apparently waits for translation to begin. This mechanism allows for synchronization of transcription and translation, a key element in attenuation.

A similar attenuation mechanism regulates the synthesis of histidine, phenylalanine and threonine.

ee also

* Trp repressor

External links

* [http://pathmicro.med.sc.edu/mayer/geneticreg.htm Mayer, Dr. Gene. Genetic Regulation at med.sc.edu]
* [http://web.indstate.edu/thcme/mwking/gene-regulation.html#trp Control of Gene Expression at indstate.edu]

References

*cite journal
title=Dynamics of synthesis, translation, and degradation of trp operon messenger RNA in E. coli.
journal=Cold Spring Harb Symp Quant Biol.
year=1969
first=DE
last=Morse
coauthors=Mosteller RD; Yanofsky C
volume=34
pages=725–40
pmid=4909527

*cite journal
title=Attenuation in the control of expression of bacterial operons
journal=Nature
year=1981
first=Charles
last=Yanofsky
volume=289
pages=751–58


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