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TRP OPERON (REPRESSIBLE SYSTEM)
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The inducible operons are activated when the substrate that is to be catabolized enters the cell. Anabolic operons function in the reverse manner: They are turned off (repressed) when their end product accumulates beyond the needs of the cell. Two entirely different, although not mutually exclusive, mechanisms seem to control the transcription of repressible operons. The rst mechanism follows the basic scheme of inducible operons and involves the end product of the pathway. The second mechanism involves secondary structure in messenger RNA transcribed from an attenuator region of the operon.
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Catabolite repression. When cAMP is present in the cell (no glucose is present), it binds with CAP protein, and together they bind to the CAP site in various sugarmetabolizing operons, such as the lac operon shown here. The CAP-cAMP complex enhances the transcription of the operon. When glucose is present, it inhibits the formation of cAMP. Thus no CAP-cAMP complex forms, and transcription of the same operons is reduced.
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One of the best-studied repressible systems is the tryptophan, or trp, operon in E. coli. The trp operon contains
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Tamarin: Principles of Genetics, Seventh Edition
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III. Molecular Genetics
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14. Gene Expression: Control in Prokaryotes and Phages
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The McGraw Hill Companies, 2001
Fourteen
Gene Expression: Control in Prokaryotes and Phages
the ve genes that code for the synthesis of the enzymes that build tryptophan, starting with chorismic acid ( g. 14.11). It has a promoter-operator sequence ( p, o) as well as its own regulator gene (trpR).
Operator Control
In this repressible system, the product of the trpR gene, the repressor, is inactive by itself; it does not recognize the operator sequence of the trp operon. The repressor only becomes active when it combines with tryptophan. Thus, when tryptophan builds up, enough is available to bind with and activate the repressor. Tryptophan is thus referred to as the corepressor. The corepressor-repressor complex then recognizes the operator, binds to it, and prevents transcription by RNA polymerase. After the available tryptophan in the cell is used up, the diffusion process causes tryptophan to leave the repressor, which then detaches from the trp operator. The transcription process no longer is blocked and can proceed normally (the operon is now derepressed). Transcription continues until enough of the various enzymes have been synthesized to again produce an excess of tryptophan. Some becomes available to bind to the repressor and make a functional complex, and the operon is again shut off and the process repeated, ensuring that tryptophan is being synthesized as needed ( g. 14.12). This regulation is modi ed, however, by the existence of the second mechanism for regulating repressible operons attenuation.
Repressed state RNA polymerase Repressor + corepressor (tryptophan)
Genes of the tryptophan operon in E. coli. The enzymes they produce control the conversion of chorismic acid to tryptophan. The symbol o on the chromosome refers to the trp operator, which has its own repressor, the product of the trpR gene.
DNA with repressor-corepressor complex
Derepressed state
DNA without repressor-corepressor complex
Inactive repressor Figure 14.12
mRNA
The repressor-corepressor complex binds at the operator and prevents the transcription of the trp operon in E. coli. Without the corepressor, the repressor cannot bind, and therefore transcription is not prevented. The blue wedge is the corepressor (two tryptophan molecules), and the partial red circle is the repressor.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
14. Gene Expression: Control in Prokaryotes and Phages
The McGraw Hill Companies, 2001
Trp Operon (Attentuator-Controlled System)
T R P O P E R O N ( AT T E N U AT O R CONTROLLED SYSTEM)
Details of the second control mechanism of repressible operons have been elucidated primarily by C. Yanofsky and his colleagues, who worked with the tryptophan operon in E. coli. This type of operon control, control by an attenuator region, has been demonstrated for at least ve other amino acid-synthesizing operons, including the leucine and histidine operons. This regulatory mechanism may be the same for most operons involved in the synthesis of an amino acid.
Charles Yanofsky (1925 ).
(Courtesy of Dr. Charles Yanofsky.)
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