Tryptophan repressor (or trp repressor) is a

transcription factor In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The fu ...

involved in controlling

amino acid Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha ...

metabolism. It has been best studied in ''

Escherichia coli ''Escherichia coli'' (),Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. also known as ''E. coli'' (), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Esc ...

'', where it is a dimeric protein that regulates transcription of the 5 genes in the tryptophan operon. When the amino acid tryptophan is plentiful in the cell, it binds to the protein, which causes a conformational change in the protein. The repressor complex then binds to its operator sequence in the genes it regulates, shutting off the genes. One of the genes regulated by trp repressor, trpR, codes for the tryptophan repressor protein itself. This is a form of feedback regulation. However, these genes are located on different operons. The (tryptophan) repressor is a 25 kD

protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, respon ...

homodimer which regulates transcription of the tryptophan biosynthetic pathway in

bacteria Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were am ...

. There are 5 operons which are regulated by trpR: the ''trpEDCBA'', ''trpR'', ''AroH'', ''AroL'', and ''mtr'' operons.

Mechanism

When the

tryptophan is in plentiful supply in the cell, trpR binds 2 molecules of tryptophan, which alters its structure and dynamics so that it becomes able to bind to operator DNA. When this occurs, transcription of the DNA is prevented, suppressing the products of the gene - proteins which make more tryptophan. When the cellular levels of tryptophan decline, the tryptophan molecules on the repressor fall off, allowing the repressor to return to its inactive form. trpR also controls the regulation of its own production, through regulation of the ''trpR'' gene. The structure of the ligand-bound holorepressor, and the ligand-free forms have been determined by both X-ray crystallography and NMR. 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 In molecular biology, RNA polymerase (abbreviated RNAP or RNApol), or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that synthesizes RNA from a DNA template. Using the enzyme helicase, RNAP locally opens the ...

can complete its reading of the strand of DNA. If the RNA polymerase reaches the terminator (at the end of the DNA strand), the enzymes for tryptophan biosynthesis are expressed.

References

{{Transcription Proteins

Mechanism

See also

References