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Intra-Allelic Complementation
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Benzer warned that certainty is elusive in the complementation test because sometimes two mutations of the same functional unit (cistron) can result in partial activity. The
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Figure 12.8 Abbreviated map of spontaneous mutations of the A and B cistrons of the rII region of T4. Each
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square represents one independently isolated mutation. Note the hot spots at A6c and B4. (From Seymour
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Benzer, On the topography of the genetic ne structure , Proceedings of the National Academy of Sciences USA 47:403 15, 1961. Reprinted by permission.)
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Tamarin: Principles of Genetics, Seventh Edition
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III. Molecular Genetics
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12. DNA: Its Mutation, Repair, and Recombination
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The McGraw Hill Companies, 2001
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DNA: Its Mutation, Repair, and Recombination
Figure 12.9 Intra-allelic complementation. With certain mutations, it is possible to get enzymatic activity
in a heterozygote for two nonfunctional alleles, if the two polypeptides form a functional enzyme. (Active site is shown in color.)
problem can be traced to the interactions of subunits at the polypeptide level. Some proteins are made up of subunits, and it is possible that certain mutant combinations produce subunits that interact to restore the enzymatic function of the protein ( g. 12.9). This phenomenon is known as intra-allelic complementation. With this in mind, geneticists routinely use the complementation test to determine functional relationships among mutations.
Colinearity
Next we look at the colinearity of the gene and the polypeptide. Benzer s work established that the gene was a linear entity, as Watson and Crick had proposed. However, Benzer could not demonstrate the colinearity of the gene and its protein product. To do this, it is necessary to show that for every mutational change in the DNA, a corresponding change takes place in the protein product of the gene. Colinearity would be established by showing that nucleotide and amino acid changes occurred in a linear fashion and in the same order in the protein and in the cistron. Ideally, Benzer himself might have solved the colinearity issue. He was halfway there, with his 350 or so isolated mutations of phage T4. However, Benzer did not have a protein product to analyze; no mutant protein had been isolated from rII mutants. In the midst of competition to nd just the right system, Charles Yanofsky of Stanford University and his colleagues emerged in the mid-1960s with the required proof, showing that the order of a polypeptide s amino acids corresponded to the nucleotide sequence in the gene that speci ed it. Yanofsky s success rested with his choice of an amenable system, one using the enzymes from a biochemical pathway. Yanofsky did his research on the tryptophan biosynthetic pathway in E. coli. The last enzyme in the pathway, tryptophan synthetase, catalyzes the reaction of indole3-glycerol-phosphate plus serine to tryptophan and
3-phosphoglyceraldehyde. The enzyme itself is made of four subunits speci ed by two separate cistrons, with each polypeptide present twice. Yanofsky and his colleagues concentrated on the A subunit. They mapped A-cistron mutations with transduction (see chapter 7) using the transducing phage P1.They rst tested each new mutant against a series of deletion mutants to establish the region where the mutation was. Then they crossed mutants for a particular region among themselves to establish relative positions and distances. The protein products of the bacterial genes were isolated using electrophoresis and chromatography to establish the ngerprint patterns of the proteins (see chapter 11). Assuming a single mutation, a comparison of the mutant and the wild-type ngerprints would show a difference of just one polypeptide spot ( g. 12.10), avoiding the need to sequence the entire protein.The mutant amino acid was
Figure 12.10 Difference in ngerprints between mutant and
wild-type polypeptide digests. The single spot that differs in the mutant can be isolated and sequenced, eliminating the need to sequence the whole protein.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
12. DNA: Its Mutation, Repair, and Recombination
The McGraw Hill Companies, 2001
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