Tryptophan repressor

Last updated
Trp repressor protein
TrpR.jpg
Ribbon diagram of the trpR protein
Identifiers
SymbolTrp_repressor
Pfam PF01371
Pfam clan CL0123
InterPro IPR000831
SCOP2 2wrp / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Trp operon repressor
Identifiers
Organism Escherichia coli
SymboltrpR
Entrez 948917
RefSeq (Prot) NP_418810
UniProt P0A881
Other data
Chromosome genome: 4.63 - 4.63 Mb
Search for
Structures Swiss-model
Domains InterPro

Tryptophan repressor (or trp repressor) is a transcription factor involved in controlling amino acid metabolism. It has been best studied in Escherichia coli , where it is a dimeric protein that regulates transcription of the 5 genes in the tryptophan operon. [1] When the amino acid tryptophan is plentiful in the cell, it binds to the protein, which causes a conformational change in the protein. [2] The repressor complex then binds to its operator sequence in the genes it regulates, shutting off the genes. [3] [4]

Contents

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 homodimer which regulates transcription of the tryptophan biosynthetic pathway in bacteria. There are 5 operons which are regulated by trpR: the trpEDCBA, trpR, AroH, AroL, and mtr operons.

Mechanism

When the amino acid 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. [5]

The structure of the ligand-bound holorepressor, and the ligand-free forms have been determined by both X-ray crystallography and NMR. [6] [7] [8] [9] [10]

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

See also

Related Research Articles

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<span class="mw-page-title-main">François Jacob</span> French biologist

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<span class="mw-page-title-main">Lac repressor</span>

The lac repressor (LacI) is a DNA-binding protein that inhibits the expression of genes coding for proteins involved in the metabolism of lactose in bacteria. These genes are repressed when lactose is not available to the cell, ensuring that the bacterium only invests energy in the production of machinery necessary for uptake and utilization of lactose when lactose is present. When lactose becomes available, it is firstly converted into allolactose by β-Galactosidase (lacZ) in bacteria. The DNA binding ability of lac repressor bound with allolactose is inhibited due to allosteric regulation, thereby genes coding for proteins involved in lactose uptake and utilization can be expressed.

<i>lac</i> operon Set genes encoding proteins and enzymes for lactose metabolism

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<span class="mw-page-title-main">Repressor</span> Sort of RNA-binding protein in molecular genetics

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<i>trp</i> operon Operon that codes for the components for production of tryptophan

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Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).

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References

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  5. Kelley RL, Yanofsky C (May 1982). "Trp aporepressor production is controlled by autogenous regulation and inefficient translation". Proc. Natl. Acad. Sci. U.S.A. 79 (10): 3120–4. Bibcode:1982PNAS...79.3120K. doi: 10.1073/pnas.79.10.3120 . PMC   346365 . PMID   7048301.
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