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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
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the A site of the ribosome, a likely event under amino acid starvation, it causes an idling reaction in the ribosome, which entails the production of the nucleotide guanosine tetraphosphate (5 -ppGpp-3 ; g. 14.37). This is part of a control mechanism called the stringent response. A protein called the stringent factor, the product of the relA gene, produces guanosine tetraphosphate (ppGpp), originally called magic spot because of its sudden appearance on chromatograms. (The gene is called rel from the relaxed mutant, which does not have the stringent response.) The stringent factor is associated with the ribosome, where ppGpp is synthesized, although it is not one of the structural proteins of the ribosome. The SpoT protein, the product of the spoT1 gene, breaks down ppGpp; thus, the concentration of ppGpp is regulated. The ppGpp interacts with RNA polymerase, causing an almost complete cessation of the transcription of ribosomal RNA; thus, no energy is wasted synthesizing ribosomes when translation is not possible. However, many amino acid-synthesizing operons require ppGpp for transcription; ppGpp thus inhibits ribosomal RNA production and enhances the production of enzymes to synthesize amino acids, all when the cell is starved for amino acids. One other thing a ribosome can do when faced with amino acid shortages is to slide past hungry codons, codons for which a charged transfer RNA is not available. At that point, the growing peptide chain will be attached to the last charged transfer RNA to enter the ribosome, the one now in the peptidyl (P) site. The complex of the transfer RNA and the ribosome slides down the messenger RNA until it encounters the next codon for the transfer RNA. At this point, it is hoped, the next codon en-
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The idling reaction. The stringent factor catalyzes the conversion of GDP to 5 -ppGpp-3 . The added pyrophosphate groups come from ATP.
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Table 14.2 Codon Distribution in MS2, an RNA Virus
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Second Position First Position U U Phe Phe Leu Leu Leu Leu Leu Leu Ile Ile Ile Met Val Val Val Val 10 13 11 4 10 14 13 6 8 16 7 15 13 12 11 10 C Ser Ser Ser Ser Pro Pro Pro Pro Thr Thr Thr Thr Ala Ala Ala Ala 13 10 10 13 7 3 6 5 14 10 8 5 19 12 14 8 A Tyr Tyr stop stop His His Gln Gln Asn Asn Lys Lys Asp Asp Glu Glu 8 13 1 1 4 4 10 16 11 23 12 17 18 11 9 14 G Cys Cys stop Trp Arg Arg Arg Arg Ser Ser Arg Arg Gly Gly Gly Gly 7 4 0 14 13 11 6 4 4 8 8 6 17 11 4 4 Third Position U C A G U C A G U C A G U C A G
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Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
14. Gene Expression: Control in Prokaryotes and Phages
The McGraw Hill Companies, 2001
Posttranslational Control
countered in the aminoacyl (A) site will code for a charged transfer RNA present.
P O S T T R A N S L AT I O N A L CONTROL
Feedback Inhibition
Even after a gene has been transcribed and the messenger RNA translated, a cell can still exert some control over the functioning of the enzymes produced if the enzymes are allosteric proteins. We have discussed the activation and deactivation of operon repressors (e.g., lac, trp) owing to their allosteric properties. Similar effects occur with other proteins. The need for posttranslational control is apparent because of the relative longevity of proteins as compared with RNA. When an operon is repressed, it no longer transcribes messenger RNA; however, the messenger RNA that was previously transcribed has been translated into protein, and this protein is still functioning. Thus, during operon repression, it would also be ef cient for the cell to control the activity of existing proteins. An example of posttranslational control occurs with the enzyme aspartate transcarbamylase, which catalyzes the rst step in the pathway of pyrimidine biosynthesis in E. coli ( g. 14.38). An excess of one of the end products of the pathway, cytidine triphosphate (CTP), inhibits the functioning of aspartate transcarbamylase.This method of control is called feedback inhibition because a product of the pathway is the agent that turns the pathway off. Aspartate transcarbamylase is an allosteric enzyme. Its active site is responsible for the condensation of carbamyl phosphate and L-aspartate ( g. 14.38). However, it also has regulatory sites that have an af nity for CTP. When CTP is bound in a regulatory site, the conformation of the enzyme changes, and the enzyme has a lowered af nity for its normal substrates; recognition of CTP inhibits the condensation reaction the enzyme normally carries out ( g. 14.39). Thus, allosteric enzymes provide a mechanism for control of protein function after the protein has been synthesized.
In recent experiments, the life span of the -galactosidase protein was determined with almost complete predictability based on its modi ed N-terminal amino acid. Protein life spans range from two minutes for those with N-terminal arginine to greater than twenty hours for those with Nterminal methionine or ve other amino acids (table 14.3). According to the PEST hypothesis, protein degradation is determined by regions rich in one of four amino acids: proline, glutamic acid, serine, and threonine. (The one-letter abbreviations of these four amino acids are P, E, S, and T, respectively.) Proteins that have these regions tend to degrade in less than 2 hours. In one study of thirty- ve proteins with half-lives of between 20 and 220 hours, only three contained a PEST region. We see that not only are different proteins programmed to survive for varying lengths of time in the cell, but that programming seems to be based on the N-terminal amino acid as well as various regions rich in the PEST amino acids.
Figure 14.38 Aspartate transcarbamylase catalyzes the rst step in pyrimidine biosynthesis. An end product, cytidine triphosphate (CTP), inhibits the enzyme.
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